(data stored in ACNUC7421 zone)

SWISSPROT: A0KF87_AERHH

ID   A0KF87_AERHH            Unreviewed;       510 AA.
AC   A0KF87;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=Histidine ammonia-lyase {ECO:0000256|HAMAP-Rule:MF_00229, ECO:0000256|RuleBase:RU004479, ECO:0000256|SAAS:SAAS00831227};
DE            Short=Histidase {ECO:0000256|HAMAP-Rule:MF_00229};
DE            EC=4.3.1.3 {ECO:0000256|HAMAP-Rule:MF_00229, ECO:0000256|RuleBase:RU004479, ECO:0000256|SAAS:SAAS00831227};
GN   Name=hutH {ECO:0000256|HAMAP-Rule:MF_00229,
GN   ECO:0000313|EMBL:ABK36958.1};
GN   OrderedLocusNames=AHA_0380 {ECO:0000313|EMBL:ABK36958.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK36958.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK36958.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidine = NH4(+) + trans-urocanate;
CC         Xref=Rhea:RHEA:21232, ChEBI:CHEBI:17771, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57595; EC=4.3.1.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00229, ECO:0000256|RuleBase:RU004479,
CC         ECO:0000256|SAAS:SAAS01124165};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00229, ECO:0000256|RuleBase:RU004479,
CC       ECO:0000256|SAAS:SAAS00765965}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229,
CC       ECO:0000256|RuleBase:RU004480, ECO:0000256|SAAS:SAAS00831222}.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO),
CC       which is formed autocatalytically by cyclization and dehydration
CC       of residues Ala-Ser-Gly. {ECO:0000256|HAMAP-Rule:MF_00229}.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO),
CC       which is formed autocatalytically by cyclization and dehydration
CC       of residues Ser-Ser-Gly. {ECO:0000256|HAMAP-Rule:MF_00229}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00229, ECO:0000256|RuleBase:RU003954,
CC       ECO:0000256|SAAS:SAAS00831225}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000462; ABK36958.1; -; Genomic_DNA.
DR   RefSeq; WP_011704356.1; NC_008570.1.
DR   RefSeq; YP_854909.1; NC_008570.1.
DR   STRING; 380703.AHA_0380; -.
DR   EnsemblBacteria; ABK36958; ABK36958; AHA_0380.
DR   GeneID; 4486964; -.
DR   KEGG; aha:AHA_0380; -.
DR   PATRIC; fig|380703.7.peg.367; -.
DR   eggNOG; ENOG4105C84; Bacteria.
DR   eggNOG; COG2986; LUCA.
DR   HOGENOM; HOG000237619; -.
DR   KO; K01745; -.
DR   OMA; CAPQVAG; -.
DR   BioCyc; AHYD380703:G1G7B-381-MONOMER; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   CDD; cd00332; PAL-HAL; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00229; His_ammonia_lyase; 1.
DR   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR005921; HutH.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR   PANTHER; PTHR10362; PTHR10362; 1.
DR   Pfam; PF00221; Lyase_aromatic; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR01225; hutH; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KF87.
DR   SWISS-2DPAGE; A0KF87.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229,
KW   ECO:0000256|SAAS:SAAS00831223};
KW   Histidine metabolism {ECO:0000256|HAMAP-Rule:MF_00229,
KW   ECO:0000256|RuleBase:RU004479, ECO:0000256|SAAS:SAAS00765967};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00229, ECO:0000256|RuleBase:RU003954,
KW   ECO:0000256|SAAS:SAAS00986691, ECO:0000313|EMBL:ABK36958.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   MOD_RES     144    144       2,3-didehydroalanine (Ser).
FT                                {ECO:0000256|HAMAP-Rule:MF_00229}.
FT   CROSSLNK    143    145       5-imidazolinone (Ala-Gly).
FT                                {ECO:0000256|HAMAP-Rule:MF_00229}.
SQ   SEQUENCE   510 AA;  54022 MW;  FFB54A7CE944ED33 CRC64;
     MFELTITPGE LDLATLRRVS REPVHVSLDP AALAGIHASA AVVTKVIEQN RVVYGINTGF
     GLLANTRIPV EQLDELQRSI VLSHAAGIGE YMDDATVRLM MVLKLNSLAR GFSGIRLVVL
     EALMRLINAE VYPVVPKKGS VGASGDLAPL AHMSCLLIGE GKARHAGELI DAATALKIAG
     LEPIALAPKE GLALLNGTQA STAFALEGLF HAEDLYAGAI TIGAMSVEAA LGSRRPFDAR
     IHAVRGQRGQ IDAAACYRHL LVDGSEIGMS HHNCEKVQDP YSLRCQPQVM GACLTQIRQA
     AEVLVCEANA VSDNPLVFAE DEDILSGGNF HAEPVAFAAD NLALAIAEIG SLSERRMALL
     IDSRMSGLPA FLVNNGGVNS GFMIAQVTSA ALASENKTLA HPASVDSLPT SANQEDHVSM
     ATFAGRRLAD MAENTRGILA VELLAAAQGL DFRAPLRSTE LIELAKGRLR EEVSFYDKDR
     YFAPDIEAAA ALLGRASYND LLPAGVLPSL
//

If you have problems or comments...

PBIL Back to PBIL home page