ID A0A099D1N9_9ACTN Unreviewed; 530 AA.
AC A0A099D1N9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:ASU77696.1};
GN ORFNames=CDG81_04515 {ECO:0000313|EMBL:ASU77696.1}, IL38_19495
GN {ECO:0000313|EMBL:KGI80088.1};
OS Actinopolyspora erythraea.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU77696.1, ECO:0000313|Proteomes:UP000215043};
RN [1] {ECO:0000313|EMBL:KGI80088.1, ECO:0000313|Proteomes:UP000029737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM90600 {ECO:0000313|EMBL:KGI80088.1,
RC ECO:0000313|Proteomes:UP000029737};
RX PubMed=25250723;
RA Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.;
RT "Identification and Characterization of a New Erythromycin Biosynthetic
RT Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-
RT Producing Halophilic Actinomycete Isolated from Salt Field.";
RL PLoS ONE 9:E108129-E108129(2014).
RN [2] {ECO:0000313|EMBL:ASU77696.1, ECO:0000313|Proteomes:UP000215043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU77696.1,
RC ECO:0000313|Proteomes:UP000215043};
RA Yin M., Tang S.;
RT "The complete genome sequence of moderately halophilic actinomycete
RT Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT novel actinopolysporins A-C and tubercidin.";
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP022752; ASU77696.1; -; Genomic_DNA.
DR EMBL; JPMV01000036; KGI80088.1; -; Genomic_DNA.
DR RefSeq; WP_052428448.1; NZ_KN214179.1.
DR AlphaFoldDB; A0A099D1N9; -.
DR KEGG; aey:CDG81_04515; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_11; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000029737; Unassembled WGS sequence.
DR Proteomes; UP000215043; 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}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 55213 MW; 840BC510BC3AB4B1 CRC64;
MRYNVEHPAT QHQVSGTTEV SPEPLTFEQV AAVARGRASV RLSERAEQGI GDTRKHIDTL
AAAEQPTYGV STGFGALAIR HIPPERRAAL QASFVRSHAA GAGDPVEPEV VRALMLLRLH
TVATGRTGVR PETAHALAAL LNSGIVPVVH EYGSLGCSGD LAPLAAVALA LTGEGEVFDA
AGARRPAAEA LPEAGIRPVT LAEKEGLALT NGTDGMLGML VLALRDLSEL VDVADVTAAM
SVEALLGTDR AFAADLQALR PHPGQARSAA RMRALLADSP VVASHRGPDC TRVQDAYSMR
CSPQVHGSAR DTVEHAATVA GRELAAAIDN PVVLGDGRVE SNGNFHGAPL AHVLDFLAIP
LADVASIAER RTDRMLDVAR SQGLPAFLAD DPGVDSGYMI AHYTQAGVVT DLKRSASPAS
VDSIPTSAMQ EDHVSMGWSA ARKLRTAVSG LRTVLAVELL TAARALDLRA PLEAAPATGA
VRDLLRTHVS GPGPDEHVAP QIRAAEQLLA SGEVHRVAAE HVDPVLGGHS
//
