ID A0A1X6Y7I3_9RHOB Unreviewed; 484 AA.
AC A0A1X6Y7I3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 ECO:0000313|EMBL:SLN12526.1};
GN ORFNames=ROH8110_00179 {ECO:0000313|EMBL:SLN12526.1};
OS Roseovarius halotolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=505353 {ECO:0000313|EMBL:SLN12526.1, ECO:0000313|Proteomes:UP000193207};
RN [1] {ECO:0000313|EMBL:SLN12526.1, ECO:0000313|Proteomes:UP000193207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8110 {ECO:0000313|EMBL:SLN12526.1,
RC ECO:0000313|Proteomes:UP000193207};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFU01000001; SLN12526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6Y7I3; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000193207; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000193207}.
FT DOMAIN 5..237
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 250..433
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 427
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 484 AA; 51145 MW; E31106064E792E54 CRC64;
MAKAIMIQGA GSNVGKSMLV AGLARAFANR GLSVAPFKPQ NMSNNAAVTP EGGEIGRAQA
LQAMAARRQP HTDMNPVLLK PESDTGAQII LQGRRFATLR AQGYADKKPQ LLTPALESFH
RLCANADLVL IEGAGSPAEI NLREGDIANM GFAEAANLPV ILIGDIDRGG VIAQIVGTQA
VLSAADAARI KAFAINKFRG DPSLFDAGMT AIEQRTGWPS LGVLPWFNDA WRLPAEDVLD
LRSSQGGGFK IAVPRLGRIA NFDDLDPLSS EPGISLVFIE PGQPLPGDAD LVLLPGSKST
IADLAHFRAQ GWDIDLRAHI RRGGHVLGLC GGYQMLGREL ADPDGIEGAP GVVAGLGHLD
VTTVMKPEKR LSMTSATYTA TGDPVAGYEI HLGETTGPDC ARAWLHLDDR PEGAASASGR
VRGTYLHGLF ASDGFRAAFL QELGVKSGLK YDSSVEDALQ SLADHVETHL DLDRILELAA
TPRA
//