ID A0A418Y9B6_9GAMM Unreviewed; 1138 AA.
AC A0A418Y9B6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Aminotransferase class V-fold PLP-dependent enzyme {ECO:0000313|EMBL:RJG36972.1};
DE Flags: Fragment;
GN ORFNames=D1Z90_20040 {ECO:0000313|EMBL:RJG36972.1};
OS Motilimonas pumila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadales genera incertae sedis; Motilimonas.
OX NCBI_TaxID=2303987 {ECO:0000313|EMBL:RJG36972.1, ECO:0000313|Proteomes:UP000283255};
RN [1] {ECO:0000313|EMBL:RJG36972.1, ECO:0000313|Proteomes:UP000283255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLHSC7-2 {ECO:0000313|EMBL:RJG36972.1,
RC ECO:0000313|Proteomes:UP000283255};
RA Wang F.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RJG36972.1, ECO:0000313|Proteomes:UP000283255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLHSC7-2 {ECO:0000313|EMBL:RJG36972.1,
RC ECO:0000313|Proteomes:UP000283255};
RA Wang F.-Q., Ren L.-H., Lin Y.-W., Sun G.-H., Du Z.-J., Zhao J.-X.,
RA Liu X.-J., Liu L.-J.;
RT "Motilimonas pumilus sp. nov., isolated from the gut of sea cucumber
RT (Apostichopus japonicus).";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50};
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:RJG36972.1}.
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DR EMBL; QZCH01000060; RJG36972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418Y9B6; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000283255; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:RJG36972.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000283255};
KW Transferase {ECO:0000313|EMBL:RJG36972.1}.
FT DOMAIN 1043..1118
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT MOD_RES 624
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RJG36972.1"
SQ SEQUENCE 1138 AA; 126351 MW; BD0570EFBF295775 CRC64;
DATALIFKDK QLSYGELNSK ANQLAHYLIN ERRVKPDTLV GICIERSPDM VVAMLGVLKS
GAAYVPLDPS YPSVRLAFML EDATLETVVT HSDLLESLPI ATTQAICLDD NITTQKLQQQ
PIDNLSREQL TLTLQHLAYV IYTSGSTGKP KGVEAPHASI INRVTWMAQQ YPAQDDEVFC
QKTAVGFVDH VAEIFQALAY GNPLVIIPTQ VSLDTARFAQ LVIEHKITRL TLVPSLLKLL
IEQNALFEMT TLRLVISSGE ALQLKEARDF YRSLPEAKLL NLYGSSEVGG DVSAYLVNAF
SGNPEVMQYF LESPHDNGLP EKPSFVPNFN YQQPPSIDAN KLFRDRYSRS ELPQMPVEYQ
DYVGQLCETI LPHVIDVTSQ RYIGHMTSKL PSFIPELNRL IARLNQNMVK VETSNSLTLI
ERQVLAMMHR LFFQLPNSFY DDNCQDPNYV FGAVTGGGSV ANMTALSYAR NRGILALGYS
QEDLVKRGAH VLLAEKGYQR AVVLGTQLMH YSMRKSVSMM GFGEDGIMYV AQDEQQKMSM
SALQRSIEYC RSNNIFIIAV VGISGATETG TVDPLAKIAA IAHENDIHFH ADAAWGGAFQ
LSPSHRSRLA GIEQADSITF CPHKMLYISQ GISLCLLKDP HGASSIATHA NYQAQKGSFD
LGQYTVEGSR PAHALLLHAS LHVLGQNGYA WLIEQSMRKT QYYTRLVQNC DSFQLVGTPD
LNIINYRYIP VSLRSASSYS VAEQQEISEV VTKIQQAQFA SGGSFASKTT IQLPNYKGGP
ITVFRIVLSN PLTTYEDLRE VLVDQLRIAN ALVEQPSNHE HNRLASLSDE AESNYAQWRV
PIGKAMRNTQ LIVLDSHLNP VPQGVFGELH VGGACVARGY HNLPALTAEK FIKNPFYDIL
KGSSSERLYK TGDLVRWLPE GELEFFGRID NQVKIRGFRI ELGEIEHALH CHEVVKSALV
LMMQSESEED ILVAYVVPCD RNNEVEQEIK TTLRTHISQL VPDYMVPAVF ILLDALPLLP
NGKVDRKRLL GLDLSEQQGE YVAPASNTED KLCAIWQKVL GVEIVGVKDN FFQLGGNSLL
ATKVLAQINL EYNTKLSLQS IFADATVSNV ASMIDALSLN SSYLVNLSTD ESLEEGLF
//
