COBQ_THEYD
ID COBQ_THEYD Reviewed; 493 AA.
AC B5YL83;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=THEYE_A1177;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-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; CP001147; ACI20228.1; -; Genomic_DNA.
DR RefSeq; WP_012544966.1; NC_011296.1.
DR RefSeq; YP_002248998.1; NC_011296.1.
DR AlphaFoldDB; B5YL83; -.
DR SMR; B5YL83; -.
DR STRING; 289376.THEYE_A1177; -.
DR EnsemblBacteria; ACI20228; ACI20228; THEYE_A1177.
DR KEGG; tye:THEYE_A1177; -.
DR PATRIC; fig|289376.4.peg.1153; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_0; -.
DR InParanoid; B5YL83; -.
DR OMA; DVRMNPL; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000718; 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..493
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090251"
FT DOMAIN 252..440
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 432
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 493 AA; 55213 MW; 4D1154CA8065BE72 CRC64;
MAKLLMIQGT SSNCGKSLIV TALCRITKNR GIKVAPFKAQ NMSLQSFITE DGGEIGLAQA
IQAEAAGVVP NVHMNPVLLK PSGQQGIQIV VHGKLYKTLN SIDFYSEKKK LWENVTDSLN
YLLKEHDFLI IEGAGSPAEI NLLEKDIVNM AVAEYLKAPV ILVGDIDRGG VFASLYGTVK
LLEKYDSLFK GFIINKFRGH VDILSPGIKK LEELINKPCL GVVPYLDETG ISDEDGVSMR
LINFFAQKVN APVKIVVLRL RYISNFNDFE PLRFEPDTEL MYSLKKEDLL SADIIIIPGS
KKTFEDLKLL RELKIDQTLR ELAKNGVEII GICGGFQMLG EKLIDPYMVE SSLREFDGIG
LLPVETLFYP EKITTQVEGC LCSEPSIKIT GYEIHKGITY GHLGLFKITR TSMNQTLFDG
IVCGNVWGTY IHGIFESDSL RRWLINRHRV KKGLNPIDYS FSWKKLKESF IDTLANTIEK
NLDINRVWEI AGL