COBQ_THEP3
ID COBQ_THEP3 Reviewed; 507 AA.
AC B0KCS6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Teth39_1900;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) 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:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; CP000924; ABY95533.1; -; Genomic_DNA.
DR RefSeq; WP_012269649.1; NC_010321.1.
DR AlphaFoldDB; B0KCS6; -.
DR SMR; B0KCS6; -.
DR STRING; 340099.Teth39_1900; -.
DR EnsemblBacteria; ABY95533; ABY95533; Teth39_1900.
DR KEGG; tpd:Teth39_1900; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002156; 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-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 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; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..507
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116436"
FT DOMAIN 249..451
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 443
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 507 AA; 57103 MW; 1FDD329578F87410 CRC64;
MTLKLMVQGT ASSVGKSLLV AAFCRIFKQD GYRVAPFKSQ NMALNSYITD EGLEIGRAQA
MQAEAAGIKP SYHMNPILLK PSSDRMSQVI LRGKVYKNIS AAEYHQFKPE LLKLIKEDFD
FLASQNDIVV IEGAGSPAEI NLRDRDVVNM GMAEMTNAPV LLVGDIDKGG VFASIAGTLL
LLKENERNRI EGVLINKFRG DIEILKPGLK MLEDIIHKKV LGVVPYMDVH IDEEDGSTER
FYRRNTEGDI EIAVINLPHI SNFTDFEPLA KIPGIKLRYV NKGERIGDCD VVIIPGTKNT
IGDLQALKEY RIDKEIFEMR KKGKFIVGIC GGYQMLGKVI KDPGRIESTT SEIEGLGLLD
IETVIENEKT TTQIKAVIRN NLPSILSPLR NIAVEGYEIH MGQSRILGDC QPFSVITHRN
GEKVEVYDGC ISDDGKVFGT YIHGIFENRE FVREFINIVR KSKGLSPIEE IIDYKEFKER
EYDKLADIVR KSIDMKEVYK IMERYRD