ID A0A0C5WLL2_9GAMM Unreviewed; 517 AA.
AC A0A0C5WLL2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=H744_1c0959 {ECO:0000313|EMBL:AJR05984.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR05984.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR05984.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR05984.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) 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:0000256|ARBA:ARBA00025166, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|ARBA:ARBA00006205, ECO:0000256|HAMAP-Rule:MF_00028}.
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DR EMBL; CP005973; AJR05984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C5WLL2; -.
DR STRING; 658445.H744_1c0959; -.
DR KEGG; pgb:H744_1c0959; -.
DR PATRIC; fig|658445.3.peg.1037; -.
DR HOGENOM; CLU_019250_2_2_6; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000032303; Chromosome 1.
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-UniRule.
DR CDD; cd05389; CobQ_N; 1.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR047045; CobQ_N.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00313; cobQ; 1.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00028};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00028};
KW Reference proteome {ECO:0000313|Proteomes:UP000032303}.
FT DOMAIN 30..255
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 276..461
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 454
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 517 AA; 56057 MW; 76DB3F1FDD5C995D CRC64;
MKMASTGRKS SGQSHSSIKR EEMQSTTKAL MVQGTTSDAG KSVLAAGLCR VLARKNIKVA
PFKSQNMALN SAVTKDGGEI GRAQAVQAQA SMIEPTVHMN PVLLKPNTDI GAQVIVQGKA
LADMDAVGYH NYKKVVLGPI MESFNILQQE YQTVIIEGAG SPAEINLREN DVANMGFAEE
ADVPVIIVAD IDRGGVFAHL YGTLALLSDS EQARVKGFVI NRFRGDIKLL ESGLDWLEQK
TGKPVLGVLP YLHGLMLEAE DAIDVQQVDA DGDQLRVSVP VLTRVSNHTD FDPLRMHPQV
NLQFIGKGQQ IPPSDLIIIP GTKSVRSDLD YLKEQGWDQQ IARHLRLGGK VMGICGGYQM
LGESIADLDG IEGEPGTSRG LGYLPIETVL APNKQLKQVR GSLTMPGQDS VPVRGYEIHA
GVTNGIDHEA PIHLADGFDG KLGIDNQVFG TYLHGIFEHK AACDAILKWA GLAATCTPDF
DLIREQGIDR VADMLEAHMD FDKLWPEWSE QLGRKGS
//