ID A0A0D6B4L5_RHOSU Unreviewed; 485 AA.
AC A0A0D6B4L5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ2 {ECO:0000313|EMBL:BAQ69745.1};
GN Synonyms=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=NHU_02597 {ECO:0000313|EMBL:BAQ69745.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ69745.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ69745.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ69745.1,
RC ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-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}.
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DR EMBL; AP014800; BAQ69745.1; -; Genomic_DNA.
DR RefSeq; WP_060835189.1; NZ_AP014800.1.
DR AlphaFoldDB; A0A0D6B4L5; -.
DR KEGG; rsu:NHU_02597; -.
DR PATRIC; fig|35806.4.peg.2674; -.
DR eggNOG; COG1492; Bacteria.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000064912; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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; 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}; Ligase {ECO:0000313|EMBL:BAQ69745.1}.
FT DOMAIN 6..238
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 254..436
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 333
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 485 AA; 51155 MW; 6DC908F41513901C CRC64;
MTARRLMVLG TGSDVGKSLL VAGLARAYAR RGLKVAPFKA QNMSNNAAVT ADGGEIGRAQ
ALQARAAGAP LSVDMNPVLV KPETDIDCQV VVRGQVRGRY SASAYQALKP DLRAEVVASL
NRLSASHDLV LIEGAGSGAE RYLRPQDISN MGLAEAADLP VVLLGDESRG GVTAAAIGHH
RLWTETERAR VRGVIVTKFR GDPGVFSPAA RDIRAETGWP VLGLLRWSEA ARALPEEDSL
GLGRRKGAGG RLVIAVPELP RIANFDDLDP LAAEAGVDLR WLRPGQPVPG DADAAILLGS
KTTRAALDAI RAEGWDIDLQ ALLRRGGRVI GLCAGYQMLG RVVRDPEGIE GPPGETPGLG
LLDIETVMTG DKRLARIEAT DRISAQPVTG YEIHMGRVAG PATARPWLDL DGTPEGAVSA
DGRVMGSHVH GLFGADGFRR HWLAGIGAGP SPEAMAGDPV ERALDRLAEE IEADLDLDAL
LTLAR
//
