ID D3PCT3_DEFDS Unreviewed; 521 AA.
AC D3PCT3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:BAI80406.1};
GN OrderedLocusNames=DEFDS_0934 {ECO:0000313|EMBL:BAI80406.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI80406.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI80406.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
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}.
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DR EMBL; AP011529; BAI80406.1; -; Genomic_DNA.
DR RefSeq; WP_013007653.1; NC_013939.1.
DR AlphaFoldDB; D3PCT3; -.
DR STRING; 639282.DEFDS_0934; -.
DR KEGG; ddf:DEFDS_0934; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_0; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000001520; Chromosome.
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:UP000001520}.
SQ SEQUENCE 521 AA; 57776 MW; C26EB72632C0EB97 CRC64;
MKTFLLGKDR LSAKKVLDIL NKELKPILDE ETYQKVNHSY QETQKVAKGE KPVYGINTGF
GPLCSTKISA DDTIKLQYNL LKSHSAGVGD FLDDNIVKTM IIIKAHALSF GYSGVQPKTI
ERMLWFLEND IIPLVPEQGS VGASGDLAPL AHLFLPLIGY GYVKYKGEIF ETGELLQKLG
IGPIELGAKE GLALINGTQF MSSFGVLSLV RMKNILENAD IIGAMTLEAL MGSLRPFDER
LHRLREYKGA LYVAHKFRTL LEGSEILKSH ENCERVQDPY SLRCIPQVHG ATWNTFLHFK
EIVHTEINSV TDNPIIFSSE DIISGGNFHG QPIALPLDYA AFSMSEIGNI SDRRTYLLLE
GNVGLPKLLM KNTGINSGFM IPQYTSAALA SENKSLCFPA SADSIPTSLG QEDHVSMGSI
SARKLYKILD NLEKILAVEL VCAAQAFDFR RPLKSGIVLE ECHKVVREYI DHADEDRIFA
NDLKKGVEII QSGKMVKAAE EIAKSKNINL YGGYYELFGI H
//
