ID A0A1Q9G6R2_9GAMM Unreviewed; 483 AA.
AC A0A1Q9G6R2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=BIT28_07650 {ECO:0000313|EMBL:OLQ69868.1};
OS Photobacterium proteolyticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1903952 {ECO:0000313|EMBL:OLQ69868.1, ECO:0000313|Proteomes:UP000186905};
RN [1] {ECO:0000313|EMBL:OLQ69868.1, ECO:0000313|Proteomes:UP000186905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13-12 {ECO:0000313|EMBL:OLQ69868.1,
RC ECO:0000313|Proteomes:UP000186905};
RA Li Y.;
RT "Photobacterium proteolyticum sp. nov. a protease producing bacterium
RT isolated from ocean sediments of Laizhou Bay.";
RL Submitted (SEP-2016) 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:OLQ69868.1}.
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DR EMBL; MJIL01000100; OLQ69868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9G6R2; -.
DR STRING; 1903952.BIT28_07650; -.
DR Proteomes; UP000186905; 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:OLQ69868.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186905}.
FT DOMAIN 24..355
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 421..474
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 483 AA; 52635 MW; A7660B0E72D113D4 CRC64;
MIDLEKNEAT LNVATRIEED LLGDRHVPAD AYWGIHTLRA VENFNISKTT ISDVPEFVRG
MVFTKKAAAM ANKELGVIPS DVGEYIVKAC DEILETGKCM DQFPSDVYQG GAGTSVNMNA
NEVIANLALE LMGKEKGEYD IVNPNDHVNK SQSTNCAYPT GFRVAVYNSI MNMVEALEYL
KGAFDAKDKE FADVLKMGRT QLQDAVPMTV GQEFHAFGVL IKEEIKNLRH TAQLLLEVNL
GATAIGTGLN AATGYQELAV QRLAEVTGLP CTPAEDLIEA TSDCGAYVMV HGALKRTAVK
LSKICNDLRL LSSGPRSGLN ELNLPEMQAG SSIMPAKVNP VIPEVVNQVC FKVIGNDTTI
TFAAEAGQLQ LNVMEPVIGQ ALFESIDLLK NASINLRDKC IDGITVNKEV CESFVFNSIG
IVTYLNPFIG HHEGDIVGKI CAETGKSVRD VVLERGLLTE AQLDDIFSVQ NLMHPEYKAK
RYN
//