ID A0A143BJ77_9BACT Unreviewed; 480 AA.
AC A0A143BJ77;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:AMW05107.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:AMW05107.1};
GN Name=aspA {ECO:0000313|EMBL:AMW05107.1};
GN ORFNames=GEMMAAP_10310 {ECO:0000313|EMBL:AMW05107.1};
OS Gemmatimonas phototrophica.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05107.1, ECO:0000313|Proteomes:UP000076404};
RN [1] {ECO:0000313|EMBL:AMW05107.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05107.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT "Functional type 2 photosynthetic reaction centers found in the rare
RT bacterial phylum Gemmatimonadetes.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN [2] {ECO:0000313|EMBL:AMW05107.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05107.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT bacteria in diverse environments.";
RL Environ. Microbiol. Rep. 8:139-149(2016).
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; CP011454; AMW05107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143BJ77; -.
DR STRING; 1379270.GEMMAAP_10310; -.
DR KEGG; gph:GEMMAAP_10310; -.
DR eggNOG; COG1027; Bacteria.
DR Proteomes; UP000076404; Chromosome.
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; PR00145; ARGSUCLYASE.
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:AMW05107.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076404}.
FT DOMAIN 17..347
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 413..465
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 480 AA; 51584 MW; 5A2F6CC4FE7CFAB1 CRC64;
MPSSPVLETR LESDPLGTLE VPADALYGIQ TVRALHNFPI SGLRPLEPFV VAQVWIKQAA
ARTHRATGRL DAQRATAIIT AADEVLAGHH RDQFVVDPYQ AGAGTSHNMN VNEVLANRAN
ELLGAARGQY APVHPNDHVN MAQSTNDTIP TNIRLAVLRQ LPALLRAVQE LSEALQDRGR
AFDGIVKAGR THLQDAMPIR LGQEFTAYAG TLERCRRRVA EAADYLNDLG IGGSAVGTGV
TVEPQYPALM VQHLREISGI PTLRVGEDRI QLMQSMGDAA AFSGALRGLA IDLSKVASDL
RLMVSGPRTG LDEISLPAVQ PGSSIMPGKI NPSIPEMVNQ VCFQVIGCDT TVTMAAEHGQ
LELNVMMPVI AHNVLLSMQL LTNAMDVLTQ KCITGIQANP AMCAYWVERS AALATALMPQ
IGYAAAAELS KRSVREGVLI RDLVKREAIL PLDQVDRVLD LRRLTEIGVP EGHHGAVTGG
//
