ID R7XZ33_9ACTN Unreviewed; 492 AA.
AC R7XZ33;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=CF8_1345 {ECO:0000313|EMBL:EON24594.1};
OS Nocardioides sp. CF8.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=110319 {ECO:0000313|EMBL:EON24594.1, ECO:0000313|Proteomes:UP000015971};
RN [1] {ECO:0000313|EMBL:EON24594.1, ECO:0000313|Proteomes:UP000015971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF8 {ECO:0000313|EMBL:EON24594.1,
RC ECO:0000313|Proteomes:UP000015971};
RX PubMed=23833136;
RA Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT of Its Metabolic Capabilities.";
RL Genome Announc. 1:e00439-e00439(2013).
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:EON24594.1}.
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; ASEP01000045; EON24594.1; -; Genomic_DNA.
DR RefSeq; WP_010832318.1; NZ_CM001852.1.
DR AlphaFoldDB; R7XZ33; -.
DR STRING; 110319.CF8_1345; -.
DR PATRIC; fig|110319.3.peg.1937; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_11; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000015971; Chromosome.
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:UP000015971}.
FT DOMAIN 5..233
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 255..427
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 492 AA; 50939 MW; 72C173B443C185BD CRC64;
MSGLLVAGTT SDAGKSVVTT GLCRAFARRG VSVAPYKAQN MSNNSMVCVA ADGTTAEIGR
AQWVQALAAK VTPEPAMNPV LLKPGSDRRS HVVLMGQPAG DVSSSDWQTG RRHLAQAAYA
AYDDLSARFE VVVAEGAGSP TEINLRASDY VNMGLARHAS TPTVVVGDID RGGVFAAMFG
TVALLDAADQ ALVAGFVVNK FRGDLDLLSP GLDSLSSLTG RRVYGVLPWD PTLWLDSEDA
LDLDGRRSDS GARCRVAVVR LPRISNFTDV DALGLEPGLD VVFAADPRDL ADADLVVLPG
TRATISDLAW LRSRGLDVAI RAHAARGRPV LGICGGFQML GASVSDPSGV EGAPGVTVDG
LGLLDVTTSF SPEKVLRLPS GTALGVDASG YEIHHGRITV GSGEAFLGGV RSGSVFGTMW
HGSLEGDELR RAFLSSALGL EPSAVSFPAA RSARLDRLGD LVEEHLDVDA LLALARSGAP
SGLPVLPPGG AA
//
