ID A0A1E4HTX8_9PSEU Unreviewed; 514 AA.
AC A0A1E4HTX8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=ABS81_24245 {ECO:0000313|EMBL:ODU00217.1};
OS Pseudonocardia sp. SCN 72-86.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1660131 {ECO:0000313|EMBL:ODU00217.1, ECO:0000313|Proteomes:UP000094542};
RN [1] {ECO:0000313|EMBL:ODU00217.1, ECO:0000313|Proteomes:UP000094542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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|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|HAMAP-Rule:MF_00028}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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:ODU00217.1}.
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DR EMBL; MEFA01000202; ODU00217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4HTX8; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000094542; 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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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 10..235
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 263..440
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 342
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 433
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 514 AA; 53530 MW; 830D5E6491C00B2B CRC64;
MSDGLTGALL VAGTTSDAGK SAVVAGLCRW LHRRGVSVAP FKAQNMSNNS VVTPDGGEIG
RAQAMQAHAC GLAPSVDFNP VLLKPGSDRT SQVVVRGRAD GHVTAMSYRT RTAALREVVA
DSLASLRARY DVVLCEGAGS PAEINLRATD ITNMGLAQAA DLPVVVVGDI DRGGVLAHLF
GTVAVLDPAD QARIAGFVVN KFRGDPALLA PGLDQLRVLT GRPTFGVLPW SDRLWLDAED
SLSAVADGVL GRPAPPRGSA WLRVAVVRLP RISNATDAEA LACEPGVAVR YATEPSRLLD
ADVVVLPGSK ATVSDLEWLR RTGMADAVLA HAAAGKPVLG ICGGYQMLGR RIADPDGVEV
AGGAVVDGLG LLDLEVRFLP EKHLGNPMGS ALGLPVRGYE IHHGRVVRSG DPVLLDDPGE
GSDTGVVLGT HWHGLLENDG FRRALLTRLA AQAGRDGFVV AGETDFAAER AAQLDVLGDL
VADHLDSAAL EHVINHGASA ELPILTTGLA ESRR
//
