ID R6WIU8_9BACT Unreviewed; 491 AA.
AC R6WIU8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
DE EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
GN ORFNames=BN725_01096 {ECO:0000313|EMBL:CDD04056.1};
OS Prevotella sp. CAG:592.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262931 {ECO:0000313|EMBL:CDD04056.1, ECO:0000313|Proteomes:UP000018343};
RN [1] {ECO:0000313|EMBL:CDD04056.1, ECO:0000313|Proteomes:UP000018343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:592 {ECO:0000313|Proteomes:UP000018343};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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,
CC 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|RuleBase:RU004479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004480}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {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:CDD04056.1}.
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DR EMBL; CBGI010000042; CDD04056.1; -; Genomic_DNA.
DR RefSeq; WP_022316620.1; NZ_FR892572.1.
DR AlphaFoldDB; R6WIU8; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000018343; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-EC.
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 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 Histidine metabolism {ECO:0000256|ARBA:ARBA00022808,
KW ECO:0000256|RuleBase:RU004479};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003954};
KW Reference proteome {ECO:0000313|Proteomes:UP000018343}.
SQ SEQUENCE 491 AA; 54039 MW; 9C7300F1A0B608F7 CRC64;
MIHKISAEHL TIERIGEIIE KGYKLELSDD ARRRIIKCRE YLDRKIAETT APVYGVTTGF
GSLCNVSVGA DQLAQLQINL MMSHACGVGD RVPNEIVKIM LLLKIQSLSY GYSGSKLDTV
ERLVDFFNND IYPIVYMQGS LGASGDLVPL AHLTLPLVGL GEVEYKGKVM TGAEVLKEMN
WQPIQLGSKE GLALLNGTQN MSAFAVWSLL QSERLSDWAD RIAAMSLDAY YGLLSPFTKA
VHVVRPHKGQ LDTAARMLEL LQGSEIAARP KPYVQDPYSF RCIPQVHGAA KDTLAYVKSV
IDTEINSATD NPTVCPDEDL IISAGNFHGE PIALPMDFLA IGMSELANIS ERRTYKLVSG
TRDLPSFLVA TPGVNSGFMI TQYTAASVVS LNKSLCTPAS VDSIPSSQGQ EDHVSMGANA
AIKLYKVVLN VERVLAIELF NAAQALEFRR PLKSSPAVEK LFEDYRKVVP FIVNDEVMYP
HIQHSIEFLR K
//
