ID A0A1S6IZ74_9FIRM Unreviewed; 505 AA.
AC A0A1S6IZ74;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=B0537_13910 {ECO:0000313|EMBL:AQS60070.1};
OS Desulforamulus ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS60070.1, ECO:0000313|Proteomes:UP000189464};
RN [1] {ECO:0000313|EMBL:AQS60070.1, ECO:0000313|Proteomes:UP000189464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSS09 {ECO:0000313|EMBL:AQS60070.1,
RC ECO:0000313|Proteomes:UP000189464};
RX PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT compost.";
RL Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
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; CP019698; AQS60070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6IZ74; -.
DR STRING; 1833852.B0537_13910; -.
DR KEGG; dfg:B0537_13910; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000189464; 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:UP000189464}.
FT DOMAIN 1..225
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 249..447
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 440
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 505 AA; 55518 MW; A002B01426A3A592 CRC64;
MLQGTSSHVG KSLLCTALCR IFWQEGFRVA PFKAQNMALN SYITLDGGEI GRAQGAQAEA
AGVVASVKMN PVLLKPKQDQ TAQVVVLGKP LADMSARDYR AKFLPEAVGL VEKCITELRQ
EYQVLVIEGA GSPAEVNLKD RDIVNMRTAF LAEAPVLLVA DIDRGGVFAA LVGTLELLEP
HERKQVAGFI INKFRGDLSL LKPGLDFLEQ RTGKPVLGVI PYLSEHGIEE EDSVALTGRL
KNQAAGELDI AVIQLPRISN FTDFDPLARV PGVALRYVGS EDNLGLPDAV IIPGTKNTLQ
DLIFLRERGL DQQIKRLVDQ GVPVVGICGG YQMLGKMLYD PWSSEATVGH LPGLGLLDME
TTFQREKQTH RCTAKLSASQ LSWGRLPHYS VMGYEIHTGE VQLGAGLKPL LEITSRSGKA
VSVSDGTVAR EGQIIGTHLH GLFDNTAFLL DWINYLRQRK NLPRLTQEQL PHMGQDKYDR
LAMLVKQHLD MKKLYEIMKL GENRA
//
