MENE_STAAN
ID MENE_STAAN Reviewed; 492 AA.
AC P63526; Q99T73;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=2-succinylbenzoate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_00731};
DE EC=6.2.1.26 {ECO:0000255|HAMAP-Rule:MF_00731};
DE AltName: Full=o-succinylbenzoyl-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731};
DE Short=OSB-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731};
GN Name=menE {ECO:0000255|HAMAP-Rule:MF_00731}; OrderedLocusNames=SA1615;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-491.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of o-succinylbenzoic acid-COA ligase from Staphylococcus
RT aureus.";
RL Submitted (AUG-2009) to the PDB data bank.
CC -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA
CC (OSB-CoA). {ECO:0000255|HAMAP-Rule:MF_00731}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-succinylbenzoate + ATP + CoA = 2-succinylbenzoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:17009, ChEBI:CHEBI:18325,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57364, ChEBI:CHEBI:456215; EC=6.2.1.26;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00731};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 5/7.
CC {ECO:0000255|HAMAP-Rule:MF_00731}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00731}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC MenE subfamily. {ECO:0000255|HAMAP-Rule:MF_00731}.
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DR EMBL; BA000018; BAB42883.1; -; Genomic_DNA.
DR PIR; E89965; E89965.
DR RefSeq; WP_000348364.1; NC_002745.2.
DR PDB; 3IPL; X-ray; 2.30 A; A/B/C=2-491.
DR PDBsum; 3IPL; -.
DR AlphaFoldDB; P63526; -.
DR SMR; P63526; -.
DR EnsemblBacteria; BAB42883; BAB42883; BAB42883.
DR KEGG; sau:SA1615; -.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OMA; WLMQRAF; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00166.
DR EvolutionaryTrace; P63526; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR HAMAP; MF_00731; MenE; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR010192; MenE.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR01923; menE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Menaquinone biosynthesis;
KW Nucleotide-binding.
FT CHAIN 1..492
FT /note="2-succinylbenzoate--CoA ligase"
FT /id="PRO_0000193168"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3IPL"
FT TURN 150..154
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3IPL"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 317..322
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 374..383
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 421..431
FT /evidence="ECO:0007829|PDB:3IPL"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 435..446
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 450..460
FT /evidence="ECO:0007829|PDB:3IPL"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:3IPL"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:3IPL"
SQ SEQUENCE 492 AA; 55357 MW; 708FB3250FADFC40 CRC64;
MDFWLYKQAQ QNGHHIAITD GQESYTYQNL YCEASLLAKR LKAYQQSRVG LYIDNSIQSI
ILIHACWLAN IEIAMINTRL TPNEMTNQMR SIDVQLIFCT LPLELRGFQI VSLDDIEFAG
RDITTNGLLD NTMGIQYDTS NETVVPKESP SNILNTSFNL DDIASIMFTS GTTGPQKAVP
QTFRNHYASA IGCKESLGFD RDTNWLSVLP IYHISGLSVL LRAVIEGFTV RIVDKFNAEQ
ILTMIKNERI THISLVPQTL NWLMQQGLHE PYNLQKILLG GAKLSATMIE TALQYNLPIY
NSFGMTETCS QFLTATPEML HARPDTVGMP SANVDVKIKN PNKEGHGELM IKGANVMNGY
LYPTDLTGTF ENGYFNTGDI AEIDHEGYVM IYDRRKDLII SGGENIYPYQ IETVAKQFPG
ISDAVCVGHP DDTWGQVPKL YFVSESDISK AQLIAYLSKH LAKYKVPKHF EKVDTLPYTS
TGKLQRNKLY RG
