ID A0A0A1DK70_NOCSI Unreviewed; 488 AA.
AC A0A0A1DK70;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 2.
DT 27-MAR-2024, entry version 38.
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=KR76_15480 {ECO:0000313|EMBL:AIY17816.2};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY17816.2, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY17816.2, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY17816.2,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
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; CP009896; AIY17816.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1DK70; -.
DR STRING; 2045.KR76_15480; -.
DR KEGG; psim:KR76_15480; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_1_11; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000030300; 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:UP000030300}.
SQ SEQUENCE 488 AA; 50816 MW; BD3334F0ECAF4BCD CRC64;
MLSDEALAAI DKARAVIEDL AASPTPHYGV STGFGALATR HIAPELRAQL QRSLVRSHAA
GSGPEVEREV VRGLMLLRLS TLATGRTGVR RETAELLAAL LSHGITPVVH EYGSLGCSGD
LAPLAHCALA LMGEGPVRTA DGELTDAATA LAAAGLTPVE LQEKEGLALI NGTDGMLGML
VLAIHDLTEL LKVADISAAM SVEGQLGTDR VFAPELQAIR PHPGQAASAA NLTTLLRDSG
VVASHRGPDC NRVQDAYSLR CSPQVHGGVR DTVAHAASVA ARELASAVDN PVVLADEGRV
ESNGNFHGAP VAYVLDFLAI VAADLASIAE RRTDRFLDKA RNHGLPPFLA DDPGVDSGLM
IAQYTQAAIV SELKRLANPA SVDSIPSSAM QEDHVSMGWS SARKLRRSVD GLTRVLAIEL
MTAARALNLR APLTPSPATG AVVELLRDAG VGGPGTDRFL APEIDTAYQL VVDRSVTAAV
TNVIGELA
//
