ID K9H5F3_9PROT Unreviewed; 514 AA.
AC K9H5F3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=C882_1635 {ECO:0000313|EMBL:EKV32797.1};
OS Caenispirillum salinarum AK4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV32797.1, ECO:0000313|Proteomes:UP000009881};
RN [1] {ECO:0000313|EMBL:EKV32797.1, ECO:0000313|Proteomes:UP000009881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK4 {ECO:0000313|EMBL:EKV32797.1,
RC ECO:0000313|Proteomes:UP000009881};
RX PubMed=23409257;
RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT AK4(T), Isolated from a Solar Saltern.";
RL Genome Announc. 1:E00199-12(2013).
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:EKV32797.1}.
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DR EMBL; ANHY01000002; EKV32797.1; -; Genomic_DNA.
DR RefSeq; WP_009538624.1; NZ_ANHY01000002.1.
DR AlphaFoldDB; K9H5F3; -.
DR STRING; 1238182.C882_1635; -.
DR PATRIC; fig|1238182.3.peg.173; -.
DR eggNOG; COG2986; Bacteria.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000009881; 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:UP000009881}.
FT MOD_RES 148
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
FT CROSSLNK 147..149
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
SQ SEQUENCE 514 AA; 53509 MW; 0BE9F3814E0EF5FF CRC64;
MTTSPDAIAL TPGGLSIDAL RRIYRDAAPI ALPDDARRRM AESRALVEQI AAGDAAVYGI
NTGFGKLAQK RIAPEDLDTL QRNLILSHAT GVGEPLDDGV VRLILASKIA SLAVGASGIR
PEVVNALLGL YHAGAMPVVP SKGSVGASGD LAPLAHLSGV LLGVGHIRIN GETVSADEGL
NRAGVERIEL KAKEGLALIN GTQVSTALAL AGLFEIERCF KAAVVSGALS VEAVKGSHKP
FDARISDLRG QPGQISVARA LRALLADSPL NASHQGEACD RVQDPYSLRC QPQVMGAVLD
QMRMAARTLR IEANGVTDNP LVLGDTGEVI SGGNFHAEPV AMAADQLAIA ASEIGALAER
RIAMLIDASI SGLPPFLVPE PGLNSGFMIA HVTAAALASE NKTLAHPASV DSLPTSANQE
DHVSMATFAA RRLRDIAGNV ADIVGIELLA AAQGLEFHRP LRSSSDMEAA LSVIRSRVPR
YEVDRYFAPD LSAIGALVRD GGLDDAVTFD LDPA
//
