ID A0A117SP64_9CREN Unreviewed; 495 AA.
AC A0A117SP64;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Probable cobyric acid synthase {ECO:0000256|ARBA:ARBA00014921, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=AT718_10500 {ECO:0000313|EMBL:KUO82280.1};
OS Vulcanisaeta sp. JCHS_4.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=1714253 {ECO:0000313|EMBL:KUO82280.1, ECO:0000313|Proteomes:UP000054689};
RN [1] {ECO:0000313|EMBL:KUO82280.1, ECO:0000313|Proteomes:UP000054689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA Inskeep W.P.;
RT "The distribution, diversity and function of predominant Thermoproteales in
RT high-temperature environments of Yellowstone National Park.";
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|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: 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:KUO82280.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LOCE01000009; KUO82280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117SP64; -.
DR STRING; 1714253.AT718_10500; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000054689; 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; 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; 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 3..239
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 250..437
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 435
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 54715 MW; 35D6672EDBBF9AEC CRC64;
MSIYLASTMS DSGKTTIVSA LLRLLRGRGL RVTPFKAQNM SLNSYPAIEG GEIALAQAMQ
AYIAGLLPSI YHNPVLIKPM DMHRAEYVIL GKPRAQLTFG QYLMDQGFRG FVVKAVKGSI
ERLRRDFDVV VGEGAGSAYE PNLANRDIAN FRPAEWLGAR VFVVLDIDRG GSFIQGLGLM
RALPPRWRRL VKGFIINKFR GDPKLLDDAI KWLESKTGKP VVGVLPYLED LWLWPEDSMD
LKPIGNGPLD IALIAYPYIS NFNDIYPLIL EDDVTVRIVR SPQELGEPHM VILPGSKNVV
ASVEWMRMTG MDKALTKIKG SVVLLGICGG FQALGKILSD PHGLEAGVPG TYRGLGFINV
NTVYGIEKVI SLSRAIGLVD GIENVEIRGY EIHRGIPQYV GDKPLVMIRE RNGRSTEQLD
GVFREDDLVI GITLHDSLGD PAFREFVLNI ARENAGLPKR RSAGLSSIDL LLRQIDKFVS
VVRDSMDIDF MVNIG
//
