ID A0A1M5DGS7_9ACTN Unreviewed; 502 AA.
AC A0A1M5DGS7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-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=SAMN05444351_0375 {ECO:0000313|EMBL:SHF66177.1};
OS Geodermatophilus nigrescens.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1070870 {ECO:0000313|EMBL:SHF66177.1, ECO:0000313|Proteomes:UP000184471};
RN [1] {ECO:0000313|EMBL:SHF66177.1, ECO:0000313|Proteomes:UP000184471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45408 {ECO:0000313|EMBL:SHF66177.1,
RC ECO:0000313|Proteomes:UP000184471};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQVX01000001; SHF66177.1; -; Genomic_DNA.
DR RefSeq; WP_073418241.1; NZ_FQVX01000001.1.
DR AlphaFoldDB; A0A1M5DGS7; -.
DR STRING; 1070870.SAMN05444351_0375; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000184471; 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:UP000184471}.
FT DOMAIN 6..228
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 257..427
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 336
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 502 AA; 52037 MW; CC1E9C85A62181E7 CRC64;
MSGALLVAGT TSDAGKSVVT AGICRWLARQ GVRVAPFKAQ NMSNNSMVTA DGAEIGRAQV
MQAQAAGVEP EAAMNPVLLK PGGDDASQVV VLGRPVAEVT ALSYRPMKAA LLEQVLASLA
DLRSRFDVVV CEGAGSPTEI NLRADDIANM GLATAAGLPV VVVGDIDRGG VFPALYGTVA
LMPPADQRLV AGFLVNKFRG DVRLLRPGLD RLTALTGRPT LGVLPWLPGA ALDVEDSLGV
PTGVSSAGPP HGEEVLRVSV ARLPRLSNFT DLDALAAEPG VLVRYATRPE ELADADLVVL
PGTRATVSDL AWLRATGLAE AVGRRAAEGR PVLGICGGHQ MLARTITDDV ESRAGTVAGL
GLLPADVSFA REKTLGRPSG EALGHPVRGY EIHHGVVTYA DGAEPFLDGG RAGAVWGTTW
HGALENDGFR RAFLAEVARA AGRRFVPAPD TSFAAVREQR LDALGDLVAE HADTAALWRL
LEEGPPDGLP LLPPGGSSGA AR
//
