ID B2A0G8_NATTJ Unreviewed; 560 AA.
AC B2A0G8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=Nther_0944 {ECO:0000313|EMBL:ACB84529.1};
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB84529.1, ECO:0000313|Proteomes:UP000001683};
RN [1] {ECO:0000313|EMBL:ACB84529.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB84529.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RX PubMed=21642468; DOI=10.1128/JB.05157-11;
RA Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA Kyrpides N., Wiegel J.;
RT "Complete genome sequence of the anaerobic, halophilic alkalithermophile
RT Natranaerobius thermophilus JW/NM-WN-LF.";
RL J. Bacteriol. 193:4023-4024(2011).
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; CP001034; ACB84529.1; -; Genomic_DNA.
DR AlphaFoldDB; B2A0G8; -.
DR STRING; 457570.Nther_0944; -.
DR KEGG; nth:Nther_0944; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_9; -.
DR InParanoid; B2A0G8; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001683; 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:UP000001683}.
FT DOMAIN 37..260
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 293..497
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 490
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 560 AA; 62278 MW; 6C3D8483F6F60047 CRC64;
MTKNFIDNNS AARNLRDRNV TDRNVDAADS DLAPCLMLQG TSSHVGKSVL VTAFCRIFSR
LGYRIAPFKA QNMANNSYVT PQGYEIGRAQ GIQAEAAQRQ ANTNMNPVLL KPSSDGTSQV
VLHGKPRGEV KAREYREDWI AFLWPQIKTA LYELRRDSDM VIIEGAGSPS EINLRDGDMA
NMSVAKEASA RVLLVSDIER GGMLASVVGT LELLPEDERD LVKGILVNKF RGDLSLLQPG
LKFLEEKTNK PVLGTLPYIK EKLVDEEDSV ALEENKNTQT NRTQGKNSRP LIKIGVVKLP
RISNFTDFEP LKEHPAVELR YLPLESKAPK LDCLIIPGTK ATLADLQEFV NSTLYVSLSE
QKQLENLPIF GICGGYQMLG LSLNDEQGIE GKAGELLGLG LLPVVTNFSP GKHTYRTALT
VNQSESSSSK NSYTFDRLFS DLKGTRLIGY EIHMGETEPV EPGYSWLIDE NNQPKGTFSQ
NGRVMGTFLH GIFNNNSFTN WFLSWVVLWN ECGSSQDFLQ KNEGYLSDME KFNILADHVE
SALDMGYISK MLNCNLQCKN
//