ID A0A088EZD6_9SPHI Unreviewed; 523 AA.
AC A0A088EZD6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=KO02_08880 {ECO:0000313|EMBL:AIM36802.1};
OS Sphingobacterium sp. ML3W.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1538644 {ECO:0000313|EMBL:AIM36802.1, ECO:0000313|Proteomes:UP000028992};
RN [1] {ECO:0000313|EMBL:AIM36802.1, ECO:0000313|Proteomes:UP000028992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML3W {ECO:0000313|EMBL:AIM36802.1};
RX PubMed=25614576;
RA Smith S.A., Krasucki S.P., McDowell J.V., Balke V.L.;
RT "Complete Genome Sequence of Sphingobacterium sp. Strain ML3W, Isolated
RT from Wings of Myotis lucifugus Infected with White Nose Syndrome.";
RL Genome Announc. 3:0-0(2015).
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; CP009278; AIM36802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A088EZD6; -.
DR STRING; 1538644.KO02_08880; -.
DR KEGG; sht:KO02_08880; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_10; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000028992; 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:UP000028992}.
SQ SEQUENCE 523 AA; 57175 MW; FF17C765131380A5 CRC64;
MITKFQYGND TMTSSLAIQL AKGETRGELT AQTIEKVVKS AQYVQEIVDS GNIVYGINTG
FGPLCTTLIS PGDTKKLQEN ILKSHAVGIG EPIDKLLSKL MLILKVHALA KGYSGIQLAT
LERILWLVEH DVIPVVPKQG SVGASGDLAP LSHLFLPLIG LGKVWYNNEI QETARVLTSF
NIQPITLGAK EGLALINGTQ FMAAHAVKAV SEMQNLLDNA DLIATLMIEG LNGSIKPFFA
QLHQLRPYKG NEYVASTIYN LLEVSEIVSS HKNCSRVQDP YSLRCIPQIH GASRHAWLHL
KDTIEIEINA VTDNPIIIDR ELTISGGSFH GQPIALPIDY ATLAISEIGN VSDRRVYLSL
EGDTPNVPKL LLKETGLNSG FMILQYSTAA LASENKGLCF PSSADSIPTS LGQEDHVSMG
SIGSRKLLQV INNVSKILSI ELICAAQAFD FHRPLRSTTI VEAVHQEIRK VIPHVKEDQI
MEEILSAAQK LISSGTLVQI ANQIADEQQV PYHGLHHEYF NVY
//
