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Database: UniProt
Entry: M0P5E6_9EURY
LinkDB: M0P5E6_9EURY
Original site: M0P5E6_9EURY 
ID   M0P5E6_9EURY            Unreviewed;       464 AA.
AC   M0P5E6;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
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   ORFNames=C461_14433 {ECO:0000313|EMBL:EMA65301.1};
OS   Halorubrum aidingense JCM 13560.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=1230454 {ECO:0000313|EMBL:EMA65301.1, ECO:0000313|Proteomes:UP000011575};
RN   [1] {ECO:0000313|EMBL:EMA65301.1, ECO:0000313|Proteomes:UP000011575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13560 {ECO:0000313|EMBL:EMA65301.1,
RC   ECO:0000313|Proteomes:UP000011575};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate
CC       groups at positions a and c of cobyrinate, using either L-glutamine or
CC       ammonia as the nitrogen source. {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 phosphate;
CC         Xref=Rhea:RHEA:26289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58537, ChEBI:CHEBI:58894,
CC         ChEBI:CHEBI:456216; EC=6.3.5.11; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00027};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00027};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 10/10. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- DOMAIN: Comprises of two domains. The C-terminal domain contains the
CC       binding site for glutamine and catalyzes the hydrolysis of this
CC       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 via
CC       a molecular tunnel, where it reacts with an activated intermediate.
CC       {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- MISCELLANEOUS: The a and c carboxylates of cobyrinate are activated for
CC       nucleophilic attack via formation of a phosphorylated intermediate by
CC       ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then
CC       that of the a-carboxylate. {ECO:0000256|HAMAP-Rule:MF_00027}.
CC   -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00027}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMA65301.1}.
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DR   EMBL; AOJI01000033; EMA65301.1; -; Genomic_DNA.
DR   RefSeq; WP_008002418.1; NZ_AOJI01000033.1.
DR   AlphaFoldDB; M0P5E6; -.
DR   STRING; 1230454.C461_14433; -.
DR   PATRIC; fig|1230454.4.peg.2906; -.
DR   OrthoDB; 8896at2157; -.
DR   UniPathway; UPA00148; UER00231.
DR   Proteomes; UP000011575; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00027; CobB_CbiA; 1.
DR   InterPro; IPR004484; CbiA_synth.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00379; cobB; 1.
DR   PANTHER; PTHR43873; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR   PANTHER; PTHR43873:SF1; COBYRINATE A,C-DIAMIDE SYNTHASE; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00027}; Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00027};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00027};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00027};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00027};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00027}.
FT   DOMAIN          6..184
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          248..454
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   REGION          217..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
FT   SITE            449
FT                   /note="Increases nucleophilicity of active site Cys"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00027"
SQ   SEQUENCE   464 AA;  47525 MW;  17777F30BF8985C1 CRC64;
     MKGVVLGGTS SGVGKTVATL ATIRALENAG HAVQPAKAGP DFVDPSHHAR VAGRPSRTLD
     LWLQGEAGLR RNYARGGGDV CVVEGVMGLY DGDESSTAAV AEALDLPVVL VVDASAGMES
     VAATALGFEA YAERAGRDVD VAGIIAQRAH GGRHERGIRE ALPDGLTYFG RIGPQEGLEI
     PERHLGLHMG EESPVGDDAL DAAAAELRTD RVVEAAREPT GAVAPTDPAE ATGAEATGTE
     ATGGDRSRVA VARDAAFRFM YPATVERLRE RAIVETFEPT AGDSLPPCDG VYLPGGYPEL
     HAEALAGSPA LADIADAAAD GVPVLGECGG LMALAESLTT VDGDTHAMAG VLPADVTMRD
     RYQALDHVEL RAKRDGPAGS TGSAASTAST ASTAPTAAAG TTLRGHEFHY SAAEVANDAR
     FAFDVVRGTG IDGAHDGLIE HRTVGTYAHV HPASGAFDAF CDGL
//
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