(data stored in ACNUC7421 zone)

SWISSPROT: C8W1Y7_DESAS

ID   C8W1Y7_DESAS            Unreviewed;       469 AA.
AC   C8W1Y7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Cobyrinate a,c-diamide synthase {ECO:0000256|HAMAP-Rule:MF_00027};
DE            EC=6.3.5.11 {ECO:0000256|HAMAP-Rule:MF_00027};
DE   AltName: Full=Cobyrinic acid a,c-diamide synthetase {ECO:0000256|HAMAP-Rule:MF_00027};
GN   Name=cbiA {ECO:0000256|HAMAP-Rule:MF_00027};
GN   OrderedLocusNames=Dtox_0078 {ECO:0000313|EMBL:ACV61041.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61041.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61041.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two
CC       carboxylate groups at positions a and c of cobyrinate, using
CC       either L-glutamine or ammonia as the nitrogen source.
CC       {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP +
CC         cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2
CC         phosphate; Xref=Rhea:RHEA:26289, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:58537,
CC         ChEBI:CHEBI:58894, ChEBI:CHEBI:456216; EC=6.3.5.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00027};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00027};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic
CC       route): step 10/10. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- DOMAIN: Comprises of two domains. The C-terminal domain contains
CC       the binding site for glutamine and catalyzes the hydrolysis of
CC       this substrate to glutamate and ammonia. The N-terminal domain is
CC       anticipated to bind ATP and cobyrinate and catalyzes the ultimate
CC       synthesis of the diamide product. The ammonia produced via the
CC       glutaminase domain is probably translocated to the adjacent domain
CC       via a molecular tunnel, where it reacts with an activated
CC       intermediate. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- MISCELLANEOUS: The a and c carboxylates of cobyrinate are
CC       activated for nucleophilic attack via formation of a
CC       phosphorylated intermediate by ATP. CbiA catalyzes first the
CC       amidation of the c-carboxylate, and then that of the a-
CC       carboxylate. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00027}.
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DR   EMBL; CP001720; ACV61041.1; -; Genomic_DNA.
DR   RefSeq; WP_012813493.1; NC_013216.1.
DR   STRING; 485916.Dtox_0078; -.
DR   EnsemblBacteria; ACV61041; ACV61041; Dtox_0078.
DR   KEGG; dae:Dtox_0078; -.
DR   eggNOG; ENOG4105C0Y; Bacteria.
DR   eggNOG; COG1797; LUCA.
DR   HOGENOM; HOG000289958; -.
DR   KO; K02224; -.
DR   OMA; MYLTNSI; -.
DR   OrthoDB; 692368at2; -.
DR   BioCyc; DACE485916:G1GFV-82-MONOMER; -.
DR   UniPathway; UPA00148; UER00231.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043775; F:cobyrinate a,c-diamide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00027; CobB_CbiA; 1.
DR   InterPro; IPR004484; CbiA_synth.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017929; CobB/CobQ_GATase.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43873; PTHR43873; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00379; cobB; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W1Y7.
DR   SWISS-2DPAGE; C8W1Y7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00027,
KW   ECO:0000256|PROSITE-ProRule:PRU00606};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00027,
KW   ECO:0000256|PROSITE-ProRule:PRU00606, ECO:0000256|SAAS:SAAS00056751};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN      259    453       GATase cobBQ-type. {ECO:0000259|PROSITE:
FT                                PS51274}.
FT   ACT_SITE    341    341       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00027}.
FT   SITE        445    445       Increases nucleophilicity of active site
FT                                Cys. {ECO:0000256|HAMAP-Rule:MF_00027}.
SQ   SEQUENCE   469 AA;  51321 MW;  8C490630A21A1A15 CRC64;
     MSSYWIPRLV IGAPQGRSGK TTVTLGILAA LTTSKKLKIQ PFKKGPDFID PSWMTQVTGR
     NCRNLDSFLM TKEDVKRAFA RGAFDADIAV VEGAMGLFDG VDIEGSGSTA EIAKAICSPV
     VLVVDATRMT RSIAALVKGF QDFDENVLIA GVILNKIARP RHENMLRAVI DHYCGIPVLG
     AIPKGQQFII PDRHLGLIPA NEDDELNLAV QKVGEAAGNY LDLDKLLEIA AGAKAIELDE
     PYISNISDDT ETSQGLKPVV GIIKDRAFSF YYPENIEAIK DAGAEIVIID ALRDKKLPYI
     NALYIGGGFP EVFAAQLQSN ESLRSDINSA VEAGMPVYAE CGGLMYLCQR LIYHGLAYDM
     VGVLPCDVQM VDKPQGHGYM IADVIDENPF FPAGAKIKGH EFHHSRVINL NYQAAKFAYR
     VERGFGIDGK NDGMIYKNVL ATYNHIHALS VKEWAANLVN RAAEYRQIP
//

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