ID A0A0X3XSY5_9ACTN Unreviewed; 502 AA.
AC A0A0X3XSY5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=ADL34_13365 {ECO:0000313|EMBL:KUL75922.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL75922.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL75922.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL75922.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-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|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:KUL75922.1}.
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DR EMBL; LLZN01000049; KUL75922.1; -; Genomic_DNA.
DR RefSeq; WP_062671277.1; NZ_LLZN01000049.1.
DR AlphaFoldDB; A0A0X3XSY5; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000052945; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000052945}.
FT DOMAIN 6..238
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 262..432
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 341
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 502 AA; 53606 MW; 12C0929C40E38EFA CRC64;
MKGGLLVAGT TSDAGKSVVT AGICRWLVRQ GVKVAPFKAQ NMSLNSFVTR EGAEIGRAQA
MQAQACRIEP TALMNPVLLK PGGDQSSQVV LLGRPVGEMS ARGYHGGRQQ RLLGTVLDSL
AELRASYDAV ICEGAGSPAE INLRRTDIVN MGIARGARLP VLVVGDIDRG GVFASFFGTV
ALLSREDQEL VAGFLVNKFR GDVSLLEPGL DMLHGLTGRR TYGVLPFRHG LGIDEEDGLR
VSLRGAVRES EVSAPVGEDV LRVAVCAVPL MSNFTDVDAL AAEPGVVVRF VDRPEELADA
DLVVVPGTRG TVRALAWLRE RGLAKALVRR AAEGRPILGV CGGFQLLGEH IEDDVESRAG
HVDGLGLLPV RVRFAREKTL TRPTGEALGE RVEGYEIHHG VAEVLAGEPF LDGCRVGQTW
GTHWHGSLES DAFRRAFLRE VAAAAGRRFV PAPGTSFAAL REEQLDRLGD LIEQHADTDA
LWRLIESGAP RGLPFISPGA PA
//
