ID I2F3W3_9BACT Unreviewed; 494 AA.
AC I2F3W3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ORFNames=Theba_0907 {ECO:0000313|EMBL:AFK06616.1};
OS Mesotoga prima MesG1.Ag.4.2.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK06616.1, ECO:0000313|Proteomes:UP000002881};
RN [1] {ECO:0000313|EMBL:AFK06616.1, ECO:0000313|Proteomes:UP000002881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mesG1.Ag.4.2 {ECO:0000313|Proteomes:UP000002881};
RX PubMed=22798451;
RA Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., Detter C.,
RA Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., Ivanova N.,
RA Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., Nesbo C.L.;
RT "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga prima
RT MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL Genome Biol. Evol. 4:700-708(2012).
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; CP003532; AFK06616.1; -; Genomic_DNA.
DR RefSeq; WP_006492613.1; NC_017934.1.
DR AlphaFoldDB; I2F3W3; -.
DR STRING; 660470.Theba_0907; -.
DR KEGG; mpg:Theba_0907; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_0; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000002881; 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:UP000002881}.
SQ SEQUENCE 494 AA; 54133 MW; 90F0AD11430D7467 CRC64;
MLIDGQHLTL SDIFEVAFKK EFCSIEESAA RLLDERRRSL ELISKEKTIY GVNTGFGVLA
DHRISSKDLD ALQKNIVLSH AAGVGEPLRQ ELVRAIMLVR ANSLLKGFSG VRKCLVQRIL
DLLNEDIVPV VPSKGSVGAS GDLAPLAHVA MSLIGEGYCT LEGSVVPSLQ ALKSRNLEPI
ILKSKEGLSL LNGTAFMAGI GGCSTYIASR LFEQAILVSA MSVDALMGST SPFDERVHSA
RPHRGQGYVA GRMKSLLEGS EIRTSHLDCD RVQDAYTLRT IPQVYGAVKD TLDYVKSVLE
IEINSATDNP LIFENGDVIS GGNFHGEPIA LAMDFLSIAL TDMGNMIERR VDRLVNPKLN
DLPAFLTNGD EGLNSGYMLW QYTAAALASE NKTLAHPASA DSIPTSGFQE DHVSMGAWGA
RKLWMIVDNL ATMISIEALL AFRALSFRHP KKSSIAVEEL FEDIRRIVPD HINDRYFGNE
FMEVRKLLFR RAGL
//