HUTH_BACSU
ID HUTH_BACSU Reviewed; 508 AA.
AC P10944;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Histidine ammonia-lyase;
DE Short=Histidase;
DE EC=4.3.1.3;
GN Name=hutH; OrderedLocusNames=BSU39350;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2454913; DOI=10.1128/jb.170.7.3199-3205.1988;
RA Oda M., Sugishita A., Furukawa K.;
RT "Cloning and nucleotide sequences of histidase and regulatory genes in the
RT Bacillus subtilis hut operon and positive regulation of the operon.";
RL J. Bacteriol. 170:3199-3205(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7704263; DOI=10.1099/13500872-141-2-337;
RA Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.;
RT "Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome
RT containing the hut and wapA loci.";
RL Microbiology 141:337-343(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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 -!- INDUCTION: By histidine.
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:0000250}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; M20659; AAA22538.1; -; Genomic_DNA.
DR EMBL; D31856; BAA06644.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15971.1; -; Genomic_DNA.
DR PIR; S18810; UFBSHS.
DR RefSeq; NP_391814.1; NC_000964.3.
DR RefSeq; WP_003243255.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P10944; -.
DR SMR; P10944; -.
DR STRING; 224308.BSU39350; -.
DR PaxDb; P10944; -.
DR PRIDE; P10944; -.
DR EnsemblBacteria; CAB15971; CAB15971; BSU_39350.
DR GeneID; 937541; -.
DR KEGG; bsu:BSU39350; -.
DR PATRIC; fig|224308.179.peg.4260; -.
DR eggNOG; COG2986; Bacteria.
DR InParanoid; P10944; -.
DR OMA; CAPQVAG; -.
DR PhylomeDB; P10944; -.
DR BioCyc; BSUB:BSU39350-MON; -.
DR BioCyc; MetaCyc:MON-11609; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000001570; 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 2: Evidence at transcript level;
KW Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT CHAIN 1..508
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000160991"
FT MOD_RES 142
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250"
FT CROSSLNK 141..143
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 508 AA; 55675 MW; 869C323BFCC318E0 CRC64;
MVTLDGSSLT TADVARVLFD FEEAAASEES MERVKKSRAA VERIVRDEKT IYGINTGFGK
FSDVLIQKED SAALQLNLIL SHACGVGDPF PECVSRAMLL LRANALLKGF SGVRAELIEQ
LLAFLNKRVH PVIPQQGSLG ASGDLAPLSH LALALIGQGE VFFEGERMPA MTGLKKAGIQ
PVTLTSKEGL ALINGTQAMT AMGVVAYIEA EKLAYQTERI ASLTIEGLQG IIDAFDEDIH
LARGYQEQID VAERIRFYLS DSGLTTSQGE LRVQDAYSLR CIPQVHGATW QTLGYVKEKL
EIEMNAATDN PLIFNDGDKV ISGGNFHGQP IAFAMDFLKI AISELANIAE RRIERLVNPQ
LNDLPPFLSP HPGLQSGAMI MQYAAASLVS ENKTLAHPAS VDSIPSSANQ EDHVSMGTIA
ARHAYQVIAN TRRVIAIEAI CALQAVEYRG IEHAASYTKQ LFQEMRKVVP SIQQDRVFSY
DIERLTDWLK KESLIPDHQN KELRGMNI
