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Database: UniProt
Entry: H3SPF1_9BACL
LinkDB: H3SPF1_9BACL
Original site: H3SPF1_9BACL 
ID   H3SPF1_9BACL            Unreviewed;       499 AA.
AC   H3SPF1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   28-FEB-2018, entry version 22.
DE   SubName: Full=5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase {ECO:0000313|EMBL:EHQ59039.1};
GN   ORFNames=PDENDC454_27308 {ECO:0000313|EMBL:EHQ59039.1};
OS   Paenibacillus dendritiformis C454.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ59039.1, ECO:0000313|Proteomes:UP000003900};
RN   [1] {ECO:0000313|EMBL:EHQ59039.1, ECO:0000313|Proteomes:UP000003900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C454 {ECO:0000313|EMBL:EHQ59039.1,
RC   ECO:0000313|Proteomes:UP000003900};
RX   PubMed=22461558; DOI=10.1128/JB.00158-12;
RA   Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA   Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V.,
RA   Nikolaev V., Gutnick D.L., Lancet D., Ben-Jacob E.;
RT   "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT   dendritiformis C454 Chiral Morphotype.";
RL   J. Bacteriol. 194:2127-2128(2012).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHQ59039.1}.
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DR   EMBL; AHKH01000181; EHQ59039.1; -; Genomic_DNA.
DR   RefSeq; WP_006679926.1; NZ_AHKH01000181.1.
DR   ProteinModelPortal; H3SPF1; -.
DR   EnsemblBacteria; EHQ59039; EHQ59039; PDENDC454_27308.
DR   PATRIC; fig|1131935.3.peg.5649; -.
DR   OrthoDB; POG091H0HWF; -.
DR   Proteomes; UP000003900; Unassembled WGS sequence.
DR   GO; GO:0018480; F:5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity; IEA:InterPro.
DR   GO; GO:1901023; P:4-hydroxyphenylacetate catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
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; IPR011985; DH_HpaE.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR02299; HpaE; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000003900};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003900}.
FT   DOMAIN       19    480       Aldedh. {ECO:0000259|Pfam:PF00171}.
SQ   SEQUENCE   499 AA;  54980 MW;  04A65DA05DD2C84C CRC64;
     MKQSHTHIGN VLHYINGQFV ESVSGRAFSN LNPFNNEPIN EVAEGFAEDI GLAVAAARQA
     FDEGPWRTMR INERMKYIIK IAELIEKYAE DISYLESLDS GLPIAQTKKQ AERAAANFRF
     YAEMVKTRLV GESYQVDNSF INYTIHKPVG VAGLITPWNA PFMLATWKVA PTLATGNTCV
     LKPAEWSPLT ANKLAEIIHE AGLPPGVFNV VHGYGETCGA PLVAHPDVQL ISFTGETTTG
     SAIIKNGSDT LKRVSMELGG KSPAIIFEDA DLDTALDAVV WQIFSFNGER CTANSRLLIH
     ESIHDPFVDR LKDRLQNIIV GDPQDPATEV GPLIHREHYN HVIRYIDTAR NEGAEVISAS
     IPQALSAGNY VAPTLILNAN NQMTVAQEEI FGPVLTVIPF STEEEALRMA NDSKYGLAGY
     VWTNDMKRGH RMAQQLECGM VWVNSQNVRD LRTPFGGTKA SGIGREGGHY GFDFYTETQI
     IHVALDEQHI PAFGKKAAR
//
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