(data stored in ACNUC7421 zone)

SWISSPROT: C7QJ65_CATAD

ID   C7QJ65_CATAD            Unreviewed;       517 AA.
AC   C7QJ65;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
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=Caci_0254 {ECO:0000313|EMBL:ACU69207.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69207.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69207.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- CATALYTIC ACTIVITY: L-histidine = urocanate + NH(3).
CC       {ECO:0000256|HAMAP-Rule:MF_00229, ECO:0000256|RuleBase:RU004479,
CC       ECO:0000256|SAAS:SAAS00765969}.
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 Cys-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; CP001700; ACU69207.1; -; Genomic_DNA.
DR   RefSeq; WP_012784502.1; NC_013131.1.
DR   ProteinModelPortal; C7QJ65; -.
DR   STRING; 479433.Caci_0254; -.
DR   EnsemblBacteria; ACU69207; ACU69207; Caci_0254.
DR   KEGG; cai:Caci_0254; -.
DR   eggNOG; ENOG4105C84; Bacteria.
DR   eggNOG; COG2986; LUCA.
DR   HOGENOM; HOG000237620; -.
DR   KO; K01745; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; POG091H04Z2; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-HAMAP.
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   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; C7QJ65.
DR   SWISS-2DPAGE; C7QJ65.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
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:SAAS00729717, ECO:0000313|EMBL:ACU69207.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   MOD_RES     145    145       2,3-didehydroalanine (Ser).
FT                                {ECO:0000256|HAMAP-Rule:MF_00229}.
FT   CROSSLNK    144    146       5-imidazolinone (Ala-Gly).
FT                                {ECO:0000256|HAMAP-Rule:MF_00229}.
SQ   SEQUENCE   517 AA;  53298 MW;  7430606240493B03 CRC64;
     MSQVVVIGEA DLTFGDVVAV ARDGARVELS ATSLKALAEG RAVVDRLAAA PTPAYGISTG
     FGALATRHID PEMRAQLQRS LIRSHAAGMG PLVEPEVIRA LTLMRLKTLA TGHTGVRPVV
     AETMAALLNS GVTPAVREYG SLGCSGDLAP LSHVALVLMG EGEVVGADGV SAVAAGPVLA
     EHGIEPLELA PKEGLALING TDGMLGMLIL ALGDLTELVK VADISAAMSV EALLGTDKVF
     RPELQAIRPH PGQAASAANL VKVLDGSPIM ESHREPNECT RVQDAYSLRC APQVAGATRD
     TMAHAATVAE RELASIVDNP VVLLADGRVE SNGNFHGAPV AMVLDFLAIA AADLGSIAER
     RTDRMLDVAR SHGLPPFLAD DPGVDSGLMI AQYTQAALVS ENKRLAVPAS VDSIPSSAMQ
     EDHVSMGWSA ARKLRTAVDN LRRILAVELV AAARALELRA PLQPAAGTGA AVRALREAGV
     GGPGPDRFLS PELRAAEDAL KSGAVVAAVE TAVGPLN
//

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