ID D4MAX8_9BACT Unreviewed; 500 AA.
AC D4MAX8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=SY1_23850 {ECO:0000313|EMBL:CBL29023.1};
OS Fretibacterium fastidiosum.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=651822 {ECO:0000313|EMBL:CBL29023.1, ECO:0000313|Proteomes:UP000008957};
RN [1] {ECO:0000313|EMBL:CBL29023.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL29023.1,
RC ECO:0000313|Proteomes:UP000008957};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Wade W., Vartoukian S.;
RT "The genome sequence of Synergistetes sp. SGP1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL29023.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL29023.1,
RC ECO:0000313|Proteomes:UP000008957};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929056; CBL29023.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MAX8; -.
DR KEGG; sbr:SY1_23850; -.
DR PATRIC; fig|651822.3.peg.1624; -.
DR HOGENOM; CLU_019250_2_2_0; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008957; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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.
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}; Ligase {ECO:0000313|EMBL:CBL29023.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008957}.
FT DOMAIN 4..235
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 252..446
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 439
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 500 AA; 54494 MW; 111AE0734E02C7F5 CRC64;
MKGIMVQGTS SDSGKSFLVT ALCRLLSDRG FRVCPFKSQN MSNNACVTRD GREMSRAQAV
QAEAARLEPE TFMNPILLKP RRDVSSEIVL EGRALDTPAE RGYYRTFTRT LGIEAVRRAL
RRIEERFDAV VIEGAGSPAE VNLNEFEIVN MRVAREADVP VVLVTDVDRG GSLASIVGTL
ELLGEDRGRV KGLIFNKFRG DRSLFDPAVV WIERRTGVPV LGVMPWVEGA AIAGEDSLNV
HWGRTGGEGL SIGVVRFPGL SNFTDLDPFE LEPDVELVGL DADTPERTLR SLDAVLLPGS
KNTMRDMAWL ERTGLARAVR ELSRAGRCVF GLCGGYQMLG ERLLDPDLKE NSEIREIEGL
GLLPSVTAFG AGEKRTVRTE GRVRRQLSAG EVPVAGYEIH FGVTHPVEGS SCPALLDVAG
GGVEGLARPD LSVAGTYLHG IFDADAFRAL WLNAVRRSRG LEERAVTDTR AMKEHAYDAL
ARAAERHLDV GAILRLMGLA
//
