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Database: UniProt
Entry: B2A0G8_NATTJ
LinkDB: B2A0G8_NATTJ
Original site: B2A0G8_NATTJ 
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
//
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