ID S4NKX1_9ACTN Unreviewed; 503 AA.
AC S4NKX1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-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=STAFG_3910 {ECO:0000313|EMBL:EPJ39044.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ39044.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ39044.1, ECO:0000313|Proteomes:UP000015001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ39044.1,
RC ECO:0000313|Proteomes:UP000015001};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) 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:EPJ39044.1}.
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DR EMBL; AOPY01001435; EPJ39044.1; -; Genomic_DNA.
DR RefSeq; WP_020272833.1; NZ_KE354189.1.
DR AlphaFoldDB; S4NKX1; -.
DR PATRIC; fig|1283301.3.peg.3879; -.
DR HOGENOM; CLU_019250_2_2_11; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000015001; 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:UP000015001}.
FT DOMAIN 7..239
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 263..432
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 426
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 503 AA; 53555 MW; 0BA88C4270A19428 CRC64;
MTGGGLLVAG TTSDAGKSVV TAGICRWLVR QGVKVAPFKA QNMSLNSFVT KEGAEIGRAQ
AMQAQACRVE PTALMNPVLL KPGGESSSQV VLLGKPVGEL SARGYHGGRQ QKLLGTVLDC
LEQLRGTYDA VICEGAGSPA EINLRRTDIV NMGIARGAGL PVLVVGDIDR GGVFASFFGT
VALLSREDQE CVAGFLVNKF RGDVSLLEPG LDMLKGLTGR PTYGVLPFRH GLGIDEEDGL
RVSLRGTVRE SVVAPPVGED VLRVAVCAVP LMSNFTDVDA LAAEPGVVVR FVDRPEELAD
ADLVIVPGTR GTVRALEWLR ERGLAEALVR RAAEQRPVLG ICGGFQILGE HIEDDVESRR
GHVEGLGVLP VRVRFAPEKT LTRPEGEALG ERVEGYEIHH GVADVTGGDP FLDGCRVGQT
WGTHWHGSLE SDGFRRAFLR GVAAAAGRRF EPAPDTSFAA LREEQLDRLG DLIEQHADTD
ALWRLIESGA PRGLPFIPPG APA
//
