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BETB2_RHIME
ID   BETB2_RHIME             Reviewed;         481 AA.
AC   Q92YD2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Betaine aldehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00804};
DE            Short=BADH 2 {ECO:0000255|HAMAP-Rule:MF_00804};
DE            EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00804};
GN   Name=betB2 {ECO:0000255|HAMAP-Rule:MF_00804}; OrderedLocusNames=RA0952;
GN   ORFNames=SMa1731;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC       betaine. Catalyzes the irreversible oxidation of betaine aldehyde to
CC       the corresponding acid. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC       Note=Binds 2 potassium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00804};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine from betaine aldehyde: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- SUBUNIT: Dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK65610.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE006469; AAK65610.1; ALT_INIT; Genomic_DNA.
DR   PIR; H95380; H95380.
DR   RefSeq; NP_436198.1; NC_003037.1.
DR   AlphaFoldDB; Q92YD2; -.
DR   SMR; Q92YD2; -.
DR   EnsemblBacteria; AAK65610; AAK65610; SMa1731.
DR   KEGG; sme:SMa1731; -.
DR   PATRIC; fig|266834.11.peg.981; -.
DR   HOGENOM; CLU_005391_0_1_5; -.
DR   UniPathway; UPA00529; UER00386.
DR   Proteomes; UP000001976; Plasmid pSymA.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_00804; BADH; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR011264; BADH.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NAD; NADP; Oxidation; Oxidoreductase; Plasmid; Potassium;
KW   Reference proteome.
FT   CHAIN           1..481
FT                   /note="Betaine aldehyde dehydrogenase 2"
FT                   /id="PRO_0000056554"
FT   ACT_SITE        164
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        286
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        460
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         29
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         96
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         152..154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         178..181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         182
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         231..234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         246
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         254
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         383
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         453
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         456
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   MOD_RES         286
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
SQ   SEQUENCE   481 AA;  51097 MW;  8C21F9C596E54988 CRC64;
     MATPLCQPAA SHFIDGTFIE DRTGPEILSV NPVDGEIIAK LHGATSCIIE KAIASAKRAQ
     KEWARKEPAE RGRVLSRAAD IMRARNRELS VLETRDTGKP ISETLVADAA SGADCLEYFG
     AIAATLSGDS IQFGEDWVYT RREPLGVCLG IGAWNYPIQI AAWKAAPALA CGNAMIFKPS
     EVTPLSALKL AEILTEAGLP PGVFNIVQGA GDVGAELATH PAIAKVSLTG SVKTGARVAS
     AAMAGIRPVT MELGGKSALI VFDDADVEAA VSGAILGNFY SAGQICSNGT RVFLQRGIRE
     AFLARLLARV AALKIGDPMD EETDIGPLVS AAHRNRVATY VARAEVEGAY QMAPPRKLPP
     GDAWHEPVVF TNVTDWMTLA REEVFGPVMA VLDFDDEQDV VARANATDFG LAAGIFTRDL
     VRAHRLAAEL EAGTVWINAY NLTPAGMAFG GIKRSGIGRE NGRVAIDHYT QLKSVFVSMQ
     T
 
 
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