COBQ_RHIWR
ID COBQ_RHIWR Reviewed; 485 AA.
AC A5VFK5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Swit_4734;
OS Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS 105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=392499;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA Richardson P.;
RT "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; CP000699; ABQ71071.1; -; Genomic_DNA.
DR RefSeq; WP_012050907.1; NC_009511.1.
DR AlphaFoldDB; A5VFK5; -.
DR SMR; A5VFK5; -.
DR STRING; 392499.Swit_4734; -.
DR EnsemblBacteria; ABQ71071; ABQ71071; Swit_4734.
DR KEGG; swi:Swit_4734; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; DVRMNPL; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001989; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..485
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332389"
FT DOMAIN 250..436
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 428
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 485 AA; 51120 MW; 9BCF7C1B1910EE80 CRC64;
MGAVMLQGTG SDVGKSVLVA GLCRAFVRRG LAVRPFKPQN MSNNAAVTID GGEIGRAQAL
QAIACRVEPH SDMNPVLLKP QADRTSQLVV HGRVRGTLGS ADFREARRPL LDEVLASYRR
LREQCDIVVV EGAGSPAEIN LRAGDIANMG FARAAGVPVV LVGDIDRGGV IAAVVGTRAV
LDPADAAMIH GFLINKFRGD PALFEDGYRQ IEALSGWRGF GVVPWLAATA RLPSEDAVIL
ERRGGPAEGR VLVACPILPR ISNFDDLDPL KLEPGVELVM VPPGRPIPAE AALIVLPGSK
ATIADLAALR AEGWDIDIRA HHRRGRAILG LCGGYQMLGR RVADPEGIEG PPGAVDGLGL
LDVETRLSPA KTLRRVEGEA LDARFDGYEM HVGETDGPGR ARPFARFDDG RTDGAIDPGG
TVMGSYVHGL LANADLRRAL LARLGIEGGG RDYAASVDAA LDAIAEEIER HVDVDALVAL
AQAGG