ID   HUTH1_FUSNN             Reviewed;         516 AA.
AC   Q8RFC2;
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 1;
DE            Short=Histidase 1;
DE            EC=4.3.1.3;
GN   Name=hutH1; OrderedLocusNames=FN0791;
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; AAL94987.1; -; Genomic_DNA.
DR   RefSeq; NP_603688.1; NC_003454.1.
DR   AlphaFoldDB; Q8RFC2; -.
DR   SMR; Q8RFC2; -.
DR   STRING; 190304.FN0791; -.
DR   PRIDE; Q8RFC2; -.
DR   EnsemblBacteria; AAL94987; AAL94987; FN0791.
DR   KEGG; fnu:FN0791; -.
DR   PATRIC; fig|190304.8.peg.1354; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_0_0; -.
DR   InParanoid; Q8RFC2; -.
DR   BioCyc; FNUC190304:G1FZS-1376-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..516
FT                   /note="Histidine ammonia-lyase 1"
FT                   /id="PRO_0000161004"
FT   MOD_RES         148
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        147..149
FT                   /note="5-imidazolinone (Ser-Gly)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   516 AA;  55978 MW;  0760ABB7CBAD0368 CRC64;
     MEVFILELVL GSKNITLEDL INVTRKGYKV SISEEAYEKI DKARALVDKY VEEGKVSYGI
     TTGFGKFAEV SISKEQTGQL QKNIVMSHSC NVGNPLPIDI AKGIVLLRAV NLAKGYSGAR
     RIVIEKLVEL LNKDVTPWIP EKGSVGSSGD LSPLAHMSLV LIGLGKAYYK GELLEAKDAL
     AKADIEPIPA LSSKEGLALT NGTQALTSTG AHVLYDAINL SKHLDIAASL TMEGLHGIID
     AYDPRIGEVR GHLGQINTAK NMRNILAGSK NVTKQGVERV QDSYVLRCIP QIHGASKDTL
     EYVKQKVELE LNAVTDNPII FVDTDEVISG GNFHGQPMAL PFDFLGIALS EMANVSERRI
     EKMVNPAINN GLPAFLVEKG GLNSGFMIVQ YSAASLVSEN KVLAHPASVD SIPTSANQED
     HVSMGSVAAK KSKDIFENVR KVIGMELITA CQAIDLKEAK DKLSPATKVA YDEVRKIISY
     VSEDRPMYID IHAAEDLIKT NKIVENVEKA IGKLEF