(data stored in ACNUC1104 zone)

SWISSPROT: E6V091_VARPE

ID   E6V091_VARPE            Unreviewed;       522 AA.
AC   E6V091;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 58.
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   OrderedLocusNames=Varpa_0183 {ECO:0000313|EMBL:ADU34405.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34405.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34405.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34405.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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}.
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DR   EMBL; CP002417; ADU34405.1; -; Genomic_DNA.
DR   RefSeq; WP_013538652.1; NC_014931.1.
DR   STRING; 595537.Varpa_0183; -.
DR   EnsemblBacteria; ADU34405; ADU34405; Varpa_0183.
DR   GeneID; 29718146; -.
DR   KEGG; vpe:Varpa_0183; -.
DR   eggNOG; ENOG4105C84; Bacteria.
DR   eggNOG; COG2986; LUCA.
DR   HOGENOM; HOG000237620; -.
DR   KO; K01745; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; 715502at2; -.
DR   BioCyc; VPAR595537:G1GQO-184-MONOMER; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000008917; 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; E6V091.
DR   SWISS-2DPAGE; E6V091.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
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:ADU34405.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917}.
FT   MOD_RES     156    156       2,3-didehydroalanine (Ser).
FT                                {ECO:0000256|HAMAP-Rule:MF_00229}.
FT   CROSSLNK    155    157       5-imidazolinone (Ala-Gly).
FT                                {ECO:0000256|HAMAP-Rule:MF_00229}.
SQ   SEQUENCE   522 AA;  53999 MW;  22A00FB19254A834 CRC64;
     MPSNNTAPTD AIDATLTLTP GKVDLAMLRR IQAGGVRLAL DPSVLDGMQK AEAAVRHIVE
     NDQVVYGINT GFGKLASTRI GNDHLAELQR NLVLSHSVGT GEPLAAPVVR MILATKAVSL
     ARGHSGVRPA LVDALLALFN AGVTPSIPCK GSVGASGDLA PLAHMACVLI GEGEATLADG
     KKVSGAEAMR SIGLEPFVLG PKEGLALLNG TQVSTALALA GLFGAEDVFA SALMSGALSL
     EAIQGSIKPF DARIHAARGQ PGQMAVAGAV RTLLEGSEIV PSHADCGRVQ DPYSVRCIPQ
     VMGACLDNLA HASRVLVIEA NAASDNPLVF CDTGEVISGG NFHAEPVAFA ADIIALAVSE
     VGAIAERRIA LLLDTGLSGL PPFLVRDGGL NSGFMIAQVT AAALASENKS LAHPASVDSL
     PTSANQEDHV SMATFAARRL GDMVNNTAVV VGIEAMAAAQ GIELKRKLKS SPLVEAEFAR
     IRQNVAFLER DRYLAPDIEA MRLWALKAEL PAALLNILPS HS
//

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