ID X7ECK8_9RHOB Unreviewed; 481 AA.
AC X7ECK8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=OCH239_08930 {ECO:0000313|EMBL:ETX13687.1};
OS Roseivivax halodurans JCM 10272.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX13687.1, ECO:0000313|Proteomes:UP000022447};
RN [1] {ECO:0000313|EMBL:ETX13687.1, ECO:0000313|Proteomes:UP000022447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX13687.1,
RC ECO:0000313|Proteomes:UP000022447};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax halodurans JCM 10272 Genome Sequencing.";
RL Submitted (JAN-2014) 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:ETX13687.1}.
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DR EMBL; JALZ01000020; ETX13687.1; -; Genomic_DNA.
DR RefSeq; WP_037264540.1; NZ_JALZ01000020.1.
DR AlphaFoldDB; X7ECK8; -.
DR STRING; 1449350.OCH239_08930; -.
DR PATRIC; fig|1449350.3.peg.3152; -.
DR eggNOG; COG1492; Bacteria.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000022447; 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:UP000022447}.
FT DOMAIN 5..237
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 252..435
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 481 AA; 50137 MW; AD3BFD2396E15540 CRC64;
MSSALMIQGT GSNVGKSMLV AGLCRAARAR GFSVAPFKPQ NMSNNAAVTA DGGEIGRAQA
LQAMACGLAP VTDMNPVLLK PETDVGAQVI VQGRRLTTTR ARDYAALKPK LLGHVLESYR
RLRAAHDLVL VEGAGSPAEV NLRANDIANM GFAAAADAPV ILAGDIDRGG VIAQIVGTQA
VMSPEDAGRV AGFLINKFRG DPSLFDDGYA MIEARTGWRG FGVLPWFPDA WRLPAEDALD
VAAPRRTEGL HIVCLQLSRI ANFDDLDPLA QEPGVRLKML APGRALPGDA DVVIVPGSKS
TRGDLAFLRA QGWDLDLAAH VRRGGHVLGI CGGYQMLGRA IADPAGIEGA PGTDPALGLL
DVETVMHADK TLTEVSARHA ASGADFTGYE IHIGRTEGPD RARPFAHVNG TPEGATGASG
RVAGSYLHGM FRDDAFRAAW LGAYGTGSDL AYDAGVEGVL DALAAHVEAH LDVGGLIAAA
R
//
