ID COBQ_CLOTE Reviewed; 491 AA.
AC Q897L4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=CTC_00720;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO35322.1; -; Genomic_DNA.
DR AlphaFoldDB; Q897L4; -.
DR SMR; Q897L4; -.
DR STRING; 212717.CTC_00720; -.
DR KEGG; ctc:CTC_00720; -.
DR HOGENOM; CLU_019250_2_2_9; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001412; 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; 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.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..491
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141298"
FT DOMAIN 249..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 491 AA; 55118 MW; C5DC91563823B6BE CRC64;
MFKLAKIMIQ GTGSSVGKSI LVTALCRIFK QDGYTVCPYK SQNMALNSYI TYDGKEMGRA
QVLQAHAAGL EPEAYMNPIL LKPTGDKKCQ IIFNGEVYGN STAMEYHNMK TKFGEKLKDQ
FKNIEEKFDI VVIEGAGSPA EINLRDKDIV NMGFAEMVDA PVLLAGDIDR GGVFASLAGT
MLLLTEEERN RVKGTIINKF RGDIEILKPG LKMLEDIIKI PTVGVVPYLK FQLEDEDGAI
DFNRNINAPI DIAVIKLPRI SNFTDFDALK VEEDVSIRYI TSKEDFGKPD LLIVPGSKNT
IEDLLALRKC GLEEKIKEYS KTGTIIGICG GYQMLGKTLK DPYKVESEEL ETQGMGLLNV
DTVFEKEKVT TRVKANSEDT EVYGYEIHMG ICNYKEGAKP LFNIYDENGK KVNRNDGAIN
EKGNVMGTYI HGVFDGVEFR EKVLNNIRKS KNMEERNAIN YENLREKNLD MLADLVRENI
DMDYIYKIIG M
//
