GenomeNet

Database: UniProt
Entry: H1HQ55_9BACT
LinkDB: H1HQ55_9BACT
Original site: H1HQ55_9BACT 
ID   H1HQ55_9BACT            Unreviewed;       470 AA.
AC   H1HQ55;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Aspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00016146, ECO:0000256|RuleBase:RU362017};
DE            Short=Aspartase {ECO:0000256|RuleBase:RU362017};
DE            EC=4.3.1.1 {ECO:0000256|ARBA:ARBA00012992, ECO:0000256|RuleBase:RU362017};
GN   ORFNames=HMPREF9944_02380 {ECO:0000313|EMBL:EHO67055.1};
OS   Segatella maculosa OT 289.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=999422 {ECO:0000313|EMBL:EHO67055.1, ECO:0000313|Proteomes:UP000003167};
RN   [1] {ECO:0000313|EMBL:EHO67055.1, ECO:0000313|Proteomes:UP000003167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT 289 {ECO:0000313|EMBL:EHO67055.1,
RC   ECO:0000313|Proteomes:UP000003167};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA   Mathney J., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella maculosa OT 289.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate = fumarate + NH4(+); Xref=Rhea:RHEA:16601,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; EC=4.3.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001494,
CC         ECO:0000256|RuleBase:RU362017};
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Aspartase subfamily. {ECO:0000256|ARBA:ARBA00005596,
CC       ECO:0000256|RuleBase:RU362017}.
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:EHO67055.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGEK01000039; EHO67055.1; -; Genomic_DNA.
DR   RefSeq; WP_008566404.1; NZ_JH594510.1.
DR   AlphaFoldDB; H1HQ55; -.
DR   STRING; 999422.HMPREF9944_02380; -.
DR   PATRIC; fig|999422.3.peg.2407; -.
DR   HOGENOM; CLU_021594_4_1_10; -.
DR   OrthoDB; 9802809at2; -.
DR   Proteomes; UP000003167; Unassembled WGS sequence.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd01357; Aspartase; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 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; IPR004708; ApsA.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR018951; Fumarase_C_C.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   NCBIfam; TIGR00839; aspA; 1.
DR   PANTHER; PTHR42696; ASPARTATE AMMONIA-LYASE; 1.
DR   PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lyase {ECO:0000256|RuleBase:RU362017, ECO:0000313|EMBL:EHO67055.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003167}.
FT   DOMAIN          14..345
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          411..463
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   COILED          201..228
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   470 AA;  51655 MW;  4B05426CBCA5F315 CRC64;
     MSEEKFRVES DLLGELKVPI NAYYGVQTQR GINNYHISRK KMRDYPDYVV AIAYVKLAAV
     QTNHSLGVIN DEISGAISQA CQEIIDGKFH EDFPIDMMQG GAGTSVNMNA NEVIANRALE
     IMGHKKGEYQ YCYPNDHVNC GQSTNDVYPT TIRLALIRMN KSLVASLTGL ISALRYKGEE
     FKDVLKMGRT QLQDAVPMTA GQEFNAYANN LEEEILNLER NIKLLHEINM GGTAIGTGLN
     AVPGFAKLCA ANLSKLTGEP FVSAIDLVEA TPDTGAYVSF SGALKRLAVK LSKICNDFRL
     MASGPRCGLN EINLPPKAPG SSIMPGKVNP VIPEVTNQVC FKVIGNDATV TFAAEAGQLE
     LNVMEPVITE CLFESLWWLH NAIDTLTEEC VLGITVNKER CYEMVKNSIG IVTALNPYIG
     YKNSTKVAKE ALETNRSVYD IVLEKGLLTK EELDEALDPK NMLASHKFIK
//
DBGET integrated database retrieval system