ID V4NQN5_9CAUL Unreviewed; 508 AA.
AC V4NQN5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
DE Short=Histidase {ECO:0000256|HAMAP-Rule:MF_00229};
DE EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
GN Name=hutH {ECO:0000256|HAMAP-Rule:MF_00229};
GN ORFNames=AEAC466_10095 {ECO:0000313|EMBL:ESQ84087.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ84087.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ84087.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ84087.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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, ECO:0000256|HAMAP-
CC Rule:MF_00229, 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|HAMAP-Rule:MF_00229,
CC ECO:0000256|RuleBase:RU004479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229,
CC ECO:0000256|RuleBase:RU004480}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000256|HAMAP-Rule:MF_00229}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000256|HAMAP-
CC Rule:MF_00229, ECO:0000256|RuleBase:RU003954}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESQ84087.1}.
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DR EMBL; AWGE01000008; ESQ84087.1; -; Genomic_DNA.
DR RefSeq; WP_023458028.1; NZ_AWGE01000008.1.
DR AlphaFoldDB; V4NQN5; -.
DR STRING; 1282362.AEAC466_10095; -.
DR PATRIC; fig|1282362.3.peg.1995; -.
DR eggNOG; COG2986; Bacteria.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000017826; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00229; His_ammonia_lyase; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229};
KW Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW Rule:MF_00229};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00229};
KW Reference proteome {ECO:0000313|Proteomes:UP000017826}.
FT MOD_RES 140
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
FT CROSSLNK 139..141
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
SQ SEQUENCE 508 AA; 53369 MW; B23ADEB144025D3D CRC64;
MILIPGQVPL SDWRRIYRGE DFRLDSACLA QVAESAAAIT RILARGEPVY GINTGFGKLA
STRIDDADLI TLQRNIILSH AAGVGAPSPR PVVRLMLALK LTSLAQGASG IRVETLTLMQ
AMLAHDLMPV IPCQGSVGAS GDLAPLAHMA ACMIGVGEID SGGVRKPALQ ALTEAGLSPL
TPGPKEGLAL LNGTQFSTAN ALAGLFEAES LLQTALITGA LSTEAAKGSD APFDPRIHAL
RRHQGQIDTA HALRTLMDGS AIRASHLKGD ERVQDPYCLR CQPQVMGAAL DVLRQAATTL
ETEANGVSDN PLIFTDPDEA LSGGNFHAEP VAFAADMIAL TLCEIGSIAE RRIAMLVDPA
LSGLPAFLTP KPGLNSGFMI PQVTAAALVS ENKQRAYPAS VDSIPTSANQ EDHVSMAAHG
ARRLMDMAEN AFAVIAIELL AAAQGCDFHA PLTSSDALER VRALTRAAVP ALDHDRHFHP
DMALAIDLVR SRAVTTAANI PLPTVEPK
//
