ID V2I348_9BURK Unreviewed; 368 AA.
AC V2I348;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833};
DE Flags: Fragment;
GN ORFNames=B551_0216590 {ECO:0000313|EMBL:ESJ07554.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ07554.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESJ07554.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-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}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|ARBA:ARBA00006205}.
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:ESJ07554.1}.
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DR EMBL; AMPR02000300; ESJ07554.1; -; Genomic_DNA.
DR AlphaFoldDB; V2I348; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000053474; Unassembled WGS sequence.
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};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00606};
KW Reference proteome {ECO:0000313|Proteomes:UP000053474}.
FT DOMAIN 10..235
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 258..367
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 348..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 368
FT /evidence="ECO:0000313|EMBL:ESJ07554.1"
SQ SEQUENCE 368 AA; 39380 MW; 1EEC036A4E3006D8 CRC64;
MPWSALRGTL MIQGTTSDAG KSTVVAGLCR LLARAAVRVV PFKPQNMALN SAVTADGGEI
GRAQALQAQA AGLASHTDMN PVLLKPSSDT GAQIIIHGRA RLDLDARAYH EYKPVAMQAV
LASHRRLCEG YDVVLVEGAG SPAEINLRER DIANMGFAEA VDCPVVLVAD IDRGGVFAHL
VGTLDCLSPS ERARVKGFII NRFRGDLSLL EPGLDWLRER TGKPVLGVLP YLHGLHLDAE
DAVAATQSAK DDGAPRLRVI VPVLPRISNH TDFDALRAHP RVDLRWIGPG TPIPPADLIV
LPGSKSVRAD LAFLREQGWE RALLRHLRYG GKVVGICGGM QMLGRRIEDP DGREGAPGGS
DGLGLLDF
//
