ID B9DPW6_STACT Unreviewed; 504 AA.
AC B9DPW6;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
DE Short=Histidase {ECO:0000256|HAMAP-Rule:MF_00229};
DE EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
GN Name=hutH {ECO:0000256|HAMAP-Rule:MF_00229,
GN ECO:0000313|EMBL:CAL29369.1};
GN OrderedLocusNames=Sca_2466 {ECO:0000313|EMBL:CAL29369.1};
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL29369.1, ECO:0000313|Proteomes:UP000000444};
RN [1] {ECO:0000313|EMBL:CAL29369.1, ECO:0000313|Proteomes:UP000000444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300 {ECO:0000313|EMBL:CAL29369.1,
RC ECO:0000313|Proteomes:UP000000444};
RX PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine = NH4(+) + trans-urocanate; Xref=Rhea:RHEA:21232,
CC ChEBI:CHEBI:17771, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595; EC=4.3.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000171, ECO:0000256|HAMAP-
CC Rule:MF_00229, ECO:0000256|RuleBase:RU004479};
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|ARBA:ARBA00005113, ECO:0000256|HAMAP-Rule:MF_00229,
CC ECO:0000256|RuleBase:RU004479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229,
CC ECO:0000256|RuleBase:RU004480}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000256|HAMAP-Rule:MF_00229}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000256|HAMAP-
CC Rule:MF_00229, ECO:0000256|RuleBase:RU003954}.
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; AM295250; CAL29369.1; -; Genomic_DNA.
DR RefSeq; WP_015901704.1; NC_012121.1.
DR AlphaFoldDB; B9DPW6; -.
DR GeneID; 60543833; -.
DR KEGG; sca:SCA_2466; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_9; -.
DR OrthoDB; 9806955at2; -.
DR BioCyc; SCAR396513:SCA_RS12390-MONOMER; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000000444; 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; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR01225; hutH; 1.
DR PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR PANTHER; PTHR10362:SF7; HISTIDINE AMMONIA-LYASE; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229};
KW Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW Rule:MF_00229};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00229}.
FT MOD_RES 143
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
FT CROSSLNK 142..144
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
SQ SEQUENCE 504 AA; 55877 MW; 4A511E7B4C19330E CRC64;
MTLELNGASL SIEDIKDFLH QQDQVAISSD ALERVKKSRA IVEDIIKNKE TIYGITTGFG
LFSDVLIDPG QYNQLQVNLI RSHACGTGDP FSHDVALVMM ILRLNTMLKG HSGVTTDLVD
QLIYFINHRI IPIIPQQGSL GASGDLAPLS HLALALIGEG KVYYQQEERE SSEVLEELGR
KPLQLSAKEG LALINGTQAM TAQGVINWIE AESLAYQSEW IASLTHQALN GITDAYRPEV
HDVRNFPEQS AVADRMLYWL EDSNLTTHQG EIRVQDAYTL RCIPQVHGAS FETLNFVKKQ
LEREMNAAND NPLIFHEDDE TLVISGGNFH GQPVAYALDF LKVAVSELGN IAERRLERLV
NPQLNGDLPA FLSPEPGLQS GAMIMQYAAA SLVSENKTLA HPASVDSIPS SANQEDHVSM
GTIASRHGYQ IADNTRRVLA IELIIALQAV ELKGIDKLSP RSREKYETLR NITPSITEDR
QFHKDITKVA RYLQQTAYTE VDCK
//
