ID A0A0M2H603_9MICO Unreviewed; 547 AA.
AC A0A0M2H603;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
DE EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
GN Name=hutH {ECO:0000313|EMBL:KJL39285.1};
GN ORFNames=RS81_02128 {ECO:0000313|EMBL:KJL39285.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL39285.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL39285.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL39285.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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,
CC 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|RuleBase:RU004479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004480}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {ECO:0000256|RuleBase:RU003954}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL39285.1}.
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DR EMBL; JYIZ01000051; KJL39285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2H603; -.
DR STRING; 92835.RS81_02128; -.
DR PATRIC; fig|92835.4.peg.2160; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000033956; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-EC.
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 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 Histidine metabolism {ECO:0000256|ARBA:ARBA00022808,
KW ECO:0000256|RuleBase:RU004479};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003954};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956}.
FT REGION 519..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 56068 MW; DD5777140FD267BC CRC64;
MTTLTETSAR DVAVVTVGSG VLSPADVVAV ARHGARVVID ASALERVAAS RALVEGLADD
PEPHYGISTG FGALATTFIA PARRAQLQAS LIRSHAAGTG PEVEREVVRA LQLLRLQTLA
TGRTGVRPVV VETYAGILNA GITPIVREYG SLGCSGDLAP LSHVALAAMG EGRVRGADGV
EVDAADALAA ASLAPLVLRE KEGLALINGT DGMLGMLLLG IHDLSMLLDT ADAAAAMSIE
SQLGTDAVFA ADLMALRPQA GQAASAANLR EFLAGSAIMA SHRDPAVCTR VQDAYSLRCS
PQVHGAARDT VDHAALIASR ELASAVDNPV ITLDGRVESN GNFHGAPVAY VLDFLAIAVA
DVASVSERRT DRALDVARNH GLPPFLADEV GVDSGLMIAQ YAAAGIVSEL KRLAAPASVD
SIPSSAMQED HVSMGWAAAR KLRRAIDGLG RVLAIEVLTA ARALDLRAPL TPAPATAAVR
DLLRGSGVAG PGPDRFLSPE MERVADLVLT GAVAGAARGA RDAASARPAA SDLPDPEEIP
DPEDATA
//
