ID A0A0F2RFD2_9PROT Unreviewed; 484 AA.
AC A0A0F2RFD2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=VR70_12605 {ECO:0000313|EMBL:KJS37363.1};
OS Rhodospirillaceae bacterium BRH_c57.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae.
OX NCBI_TaxID=1629718 {ECO:0000313|EMBL:KJS37363.1, ECO:0000313|Proteomes:UP000033468};
RN [1] {ECO:0000313|EMBL:KJS37363.1, ECO:0000313|Proteomes:UP000033468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c57 {ECO:0000313|EMBL:KJS37363.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJS37363.1}.
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DR EMBL; LAEA01000173; KJS37363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2RFD2; -.
DR STRING; 1629718.VR70_12605; -.
DR PATRIC; fig|1629718.3.peg.3940; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000033468; Unassembled WGS sequence.
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}.
FT DOMAIN 6..238
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 256..436
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 430
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 484 AA; 50816 MW; 367DC26A39756E2B CRC64;
MTARSLMFQG TGSDVGKSLL VAGLARAYTR RGLRVLPFKP QNMSNNAAVT ADGGEIGRAQ
ALQALAAGVA PTVHMNPVLL KPQSHIGAQV VVQGKVRGSR SAAEFQGLKA GLMEAVQDSF
ARLRSEADLV LIEGAGSAAE VNLRRNDIAN MGFARAADVP VVLIGDIDRG GVIASIVGTQ
AVLDPADAAM VVGFVINKFR GDPNLFSEGM EIIATRTGWQ ALGLVPHFAA AARLPAEDAV
ALTHARRGTK DGARITVAVP ILPCIANFDD LDPLEAEPGV EVIHLRPGMT LPTDTTLVLL
PGSKSTVADL KALREHGWDI DILAHARRGG WVMGLCGGYQ MLGHRVEDPE GVEGPAGGVD
ALGLLDVTTV LSADKRLAPA RGATFDGVAF TGYEMHMGRT TGPDTAHPFA QLAEGPEGAV
SGRIFGSYVH GLFADDAQRS AWLTRLGGGA AEISYDRQIQ DTLDALADHL EAHMPLTRLL
ELAR
//
