ID N8Y7P9_9GAMM Unreviewed; 483 AA.
AC N8Y7P9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=F960_02967 {ECO:0000313|EMBL:ENV32792.1};
OS Acinetobacter gerneri DSM 14967 = CIP 107464 = MTCC 9824.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120926 {ECO:0000313|EMBL:ENV32792.1, ECO:0000313|Proteomes:UP000013117};
RN [1] {ECO:0000313|EMBL:ENV32792.1, ECO:0000313|Proteomes:UP000013117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107464 {ECO:0000313|EMBL:ENV32792.1,
RC ECO:0000313|Proteomes:UP000013117};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter gerneri CIP 107464.";
RL Submitted (FEB-2013) 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:ENV32792.1}.
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; APPN01000072; ENV32792.1; -; Genomic_DNA.
DR RefSeq; WP_004865994.1; NZ_KB849544.1.
DR AlphaFoldDB; N8Y7P9; -.
DR STRING; 202952.GCA_000747725_00191; -.
DR GeneID; 84210262; -.
DR PATRIC; fig|1120926.3.peg.2877; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_0_6; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000013117; 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; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU362017, ECO:0000313|EMBL:ENV32792.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013117}.
FT DOMAIN 18..350
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 416..468
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 483 AA; 52681 MW; 7F41BC093FECB41E CRC64;
METVQAAKTR IEKDLLGAKE VPVDCYYGIH TLRALENFKI STHTVGEQLH FIRALAQVKK
ASAQANLKFG KISEQISEAI QRACDELIAQ PENWGSSFPS DVFQGGAGTS INMNTNEVIA
NIALGYLGYE KGSYSIIHPN DHVNKSQSTN DVYPTALRLA TFYALDGLIQ QMNKLIHSII
DKSVEFQNVL KMGRTQLQDA VPMTLGQEFH AFATLLKEDV RLIQRTRNLL LEINLGATAI
GTGVNTPHGY AAEVGENLKQ ITGLNLTGAE DYVEATSDCG VFIILSSTLK RLAVKLSKIC
NDLRLLSSGP RTGLGEIRLP ELQAGSSIMP AKVNPVIPEV VNQIAFKVIG NDLTITFAAE
AGQLQLNVME PVIAVSINES INLLINGIQS LDEKCIQGIE ANVQSCHDAV MRSVGIVTLL
DPILGHAKCD EIGKLCIAQN KTIQEVVLEQ NLLSKEQMDE IFSFENLVSA IAVRPYEEMN
QVG
//
