GNGF_ALKHC
ID GNGF_ALKHC Reviewed; 322 AA.
AC Q9K706;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Gluconeogenesis factor {ECO:0000255|HAMAP-Rule:MF_00973};
GN OrderedLocusNames=BH3568;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-322.
RA Kuzin A.P., Chen Y., Seetharaman J., Benach J., Shastry R., Conover K.,
RA Ma L.C., Xiao R., Liu J., Baran M.C., Acton T.B., Rost B., Montelione G.T.,
RA Hunt J.F., Tong L.;
RT "X-ray structure of the hypothetical UPF0052 protein BH3568 from Bacillus
RT halodurans.";
RL Submitted (AUG-2006) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-322 IN COMPLEX WITH NAD.
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of hypothetical protein (NP_244435.1) from Bacillus
RT halodurans at 2.60 A resolution.";
RL Submitted (NOV-2006) to the PDB data bank.
CC -!- FUNCTION: Required for morphogenesis under gluconeogenic growth
CC conditions. {ECO:0000255|HAMAP-Rule:MF_00973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00973}.
CC -!- SIMILARITY: Belongs to the gluconeogenesis factor family.
CC {ECO:0000255|HAMAP-Rule:MF_00973}.
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DR EMBL; BA000004; BAB07287.1; -; Genomic_DNA.
DR PIR; H84095; H84095.
DR RefSeq; WP_010899696.1; NC_002570.2.
DR PDB; 2HZB; X-ray; 2.80 A; A/B/C/D=1-322.
DR PDB; 2O2Z; X-ray; 2.60 A; A/B/C/D=1-322.
DR PDBsum; 2HZB; -.
DR PDBsum; 2O2Z; -.
DR AlphaFoldDB; Q9K706; -.
DR SMR; Q9K706; -.
DR STRING; 272558.10176192; -.
DR EnsemblBacteria; BAB07287; BAB07287; BAB07287.
DR KEGG; bha:BH3568; -.
DR eggNOG; COG0391; Bacteria.
DR HOGENOM; CLU_044041_0_1_9; -.
DR OMA; LCGDDDW; -.
DR OrthoDB; 665169at2; -.
DR EvolutionaryTrace; Q9K706; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10680; -; 1.
DR HAMAP; MF_00973; Gluconeogen_factor; 1.
DR InterPro; IPR002882; CofD.
DR InterPro; IPR038136; CofD-like_dom_sf.
DR InterPro; IPR010119; Gluconeogen_factor.
DR PANTHER; PTHR30135; PTHR30135; 1.
DR Pfam; PF01933; CofD; 1.
DR SUPFAM; SSF142338; SSF142338; 1.
DR TIGRFAMs; TIGR01826; CofD_related; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NAD; Reference proteome.
FT CHAIN 1..322
FT /note="Gluconeogenesis factor"
FT /id="PRO_0000107803"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 217..219
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 263..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 300..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2HZB"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2O2Z"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:2O2Z"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2O2Z"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:2O2Z"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:2O2Z"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:2O2Z"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:2O2Z"
SQ SEQUENCE 322 AA; 34436 MW; F9E320F0B467208D CRC64;
MKKKNVVVFG GGTGLSVLLR GLKTFPVSIT AIVTVADDGG SSGRLRKELD IPPPGDVRNV
LVALSEVEPL LEQLFQHRFE NGNGLSGHSL GNLLLAGMTS ITGDFARGIS EMSKVLNVRG
KVLPASNRSI ILHGEMEDGT IVTGESSIPK AGKKIKRVFL TPKDTKPLRE GLEAIRKADV
IVIGPGSLYT SVLPNLLVPG ICEAIKQSTA RKVYICNVMT QNGETDGYTA SDHLQAIMDH
CGVGIVDDIL VHGEPISDTV KAKYAKEKAE PVIVDEHKLK ALGVGTISDY FVLEQDDVLR
HNASKVSEAI LEGKPRTSSS IQ
