ID   HUTH2_FUSNN             Reviewed;         511 AA.
AC   Q8RDU4;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Histidine ammonia-lyase 2;
DE            Short=Histidase 2;
DE            EC=4.3.1.3;
GN   Name=hutH2; OrderedLocusNames=FN1406;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC       is formed autocatalytically by cyclization and dehydration of residues
CC       Ser-Ser-Gly. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR   EMBL; AE009951; AAL95599.1; -; Genomic_DNA.
DR   RefSeq; NP_604300.1; NC_003454.1.
DR   AlphaFoldDB; Q8RDU4; -.
DR   SMR; Q8RDU4; -.
DR   STRING; 190304.FN1406; -.
DR   EnsemblBacteria; AAL95599; AAL95599; FN1406.
DR   KEGG; fnu:FN1406; -.
DR   PATRIC; fig|190304.8.peg.1967; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_0; -.
DR   InParanoid; Q8RDU4; -.
DR   OMA; CAPQVAG; -.
DR   BioCyc; FNUC190304:G1FZS-1977-MON; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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; 1.10.275.10; -; 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   PANTHER; PTHR10362; PTHR10362; 1.
DR   Pfam; PF00221; Lyase_aromatic; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR01225; hutH; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT   CHAIN           1..511
FT                   /note="Histidine ammonia-lyase 2"
FT                   /id="PRO_0000161005"
FT   MOD_RES         145
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        144..146
FT                   /note="5-imidazolinone (Ser-Gly)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  55498 MW;  B0B17DE55B54EAE2 CRC64;
     MQKIIEINGS NLTIEDVVAV ARYGAKVKLD EKQKDKILES RKYVEEALSN KMPIYGINTG
     FGKFENVPIS EEELELLQKN LIYSDACGVG EAFDTEIVRA MMILRANAIS KGFSGVMIET
     VECLLNMLNA GVHPIVRSKG SVGSSGDLCP LAHMVLPMIG EGEAEYKGEI LSGKEAMKKA
     GVSTITLKAK EGLALINGTQ AMMGNAVLAV YDAEKLLKQA DIVASLSIDA LGGIIDAFDE
     RIHLIRPHKG QIYSAENLRK LLKGSKRTTR QGEKRMQDAY SLRCTPQVHG ASRLAFDYVK
     QTVETEINSV TDNPLIFPGE NGACISGGNF HGQPIAIAMD TLGILMSEIA NISERRIEKL
     VNPALSHGLP AFLVKNGGIN DGFMIPQYVA AALVSENKVL AHPASVDSIP TSANQEDHVS
     MGTIGARKAR TIVDHAQHVV SIELLCAAQA ADFWDSKNLG VGTKEAYRTL REKVDFMEND
     VIFYPLMDKS FEIIKSAILL ANVEKIIGLL K