COBQ_DESVV
ID COBQ_DESVV Reviewed; 539 AA.
AC A1VFG1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Dvul_2161;
OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=391774;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP4;
RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA Stahl D.A.;
RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT plasticity.";
RL Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM29177.1; -; Genomic_DNA.
DR RefSeq; WP_011792694.1; NC_008751.1.
DR AlphaFoldDB; A1VFG1; -.
DR EnsemblBacteria; ABM29177; ABM29177; Dvul_2161.
DR KEGG; dvl:Dvul_2161; -.
DR HOGENOM; CLU_019250_2_2_7; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000009173; 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.
FT CHAIN 1..539
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002356"
FT DOMAIN 260..483
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 346
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 475
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 539 AA; 56462 MW; 89E38330DB0A4F7B CRC64;
MKSPTPALML QGTSSNAGKS ILTAAFCRIL LQDGYRVAPF KAQNMALNSH VTADGLELGR
AQAVQAAACR LDVDVRMNPV LLKPNSDTGS QVVVMGRPVG NMRVREYMAY KPVAFDAARA
AYDSLAADVD VMVLEGAGSP AEVNLKAHDI VNMAMARHAE AKVLLVGDID RGGVFASLVG
TMELLDPWER DLVAGFVLNK FRGDATLLSP AYDVVTGRTG KPFLGVVPWL HDLGLPDEDS
VSFRETLAGR APDVPAGGGM LDIVLVDLPH ISNFTDLDAL RREPDVAVRV VRSPEQLGSP
DAIILPGSKN TLGDLAALRS RGMAEALCAL RSADGGHLGP VIVGICGGFQ MMGRLLADPQ
GVESDHARTE AGLGLLPVTT EMGSAKVLRR TSAKTVSGWC GAGVAAGLMP GTGGGHGGAE
ACPGEGYAVH GYEIHHGVTT PDAGGGAVLV CLHESDGSPA GWTTPDGQVW GTYLHGVFDA
DGFRRGWLDA LRVRRGLEPV GRIVARYDLD PALDRLADAV RGAVDMTHVY SLLGLPPQG
