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Database: UniProt
Entry: W1RZY4_9GAMM
LinkDB: W1RZY4_9GAMM
Original site: W1RZY4_9GAMM 
ID   W1RZY4_9GAMM            Unreviewed;       467 AA.
AC   W1RZY4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:ETI61284.1};
DE            EC=4.3.1.1 {ECO:0000313|EMBL:ETI61284.1};
GN   Name=aspA {ECO:0000313|EMBL:ETI61284.1};
GN   ORFNames=D104_06165 {ECO:0000313|EMBL:ETI61284.1};
OS   Marinomonas profundimaris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=1208321 {ECO:0000313|EMBL:ETI61284.1, ECO:0000313|Proteomes:UP000018857};
RN   [1] {ECO:0000313|EMBL:ETI61284.1, ECO:0000313|Proteomes:UP000018857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D104 {ECO:0000313|EMBL:ETI61284.1,
RC   ECO:0000313|Proteomes:UP000018857};
RX   PubMed=24459272;
RA   Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT   "Draft Genome Sequence of Marinomonas sp. Strain D104, a Polycyclic
RT   Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT   Arctic Ocean.";
RL   Genome Announc. 2:0-0(2014).
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:ETI61284.1}.
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DR   EMBL; AYOZ01000008; ETI61284.1; -; Genomic_DNA.
DR   RefSeq; WP_024023396.1; NZ_AYOZ01000008.1.
DR   AlphaFoldDB; W1RZY4; -.
DR   STRING; 1208321.D104_06165; -.
DR   PATRIC; fig|1208321.3.peg.1222; -.
DR   eggNOG; COG1027; Bacteria.
DR   OrthoDB; 9802809at2; -.
DR   Proteomes; UP000018857; Unassembled WGS sequence.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
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; 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   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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:ETI61284.1}.
FT   DOMAIN          11..341
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          408..460
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   467 AA;  50079 MW;  F35EF9BD71C038E6 CRC64;
     MNTRSEYDLL GNMDIPVDAL YGIQTQRAAQ NFSITGIPIS HFPELIKALA MVKAAAARTN
     QEMKLLTAEK ADAIVFACQD LILGKHHDQF IVDVIQGGAG TSTNMNANEV IANIALLKLG
     HEKGEYKYLH PNDDVNRSQS TNDAYPTAAC LGIQFAADNF LPSLASLKEA LETKACEFSH
     IVKMGRTQLQ DAVPMTLGQE FDAFAVTLGE DIDRIREACT LLCEVNLGGT AIGTGINTPE
     GYSKIVVEKL ATISTKPLVS ASNLVEATSD MGAFVFFSGI LKRLAIKLSK MSNDLRLLSS
     GPRTGLGEIN LPPMQPGSSI MPGKVNPVIP EAMNQTAYQV IASDLAVTLA AESGQLQLNA
     MEPMIIYNVL NSLKMLKEAC QMLETRCIRG ITANEAVCAG HVENSIGIIT ALVPHIGYAN
     ASRIANTALH TGNTVKALVI EENLLTEEQV NILLSPQSML SPSKVVI
//
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