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Database: UniProt
Entry: A0A367RIX1_9NOSO
LinkDB: A0A367RIX1_9NOSO
Original site: A0A367RIX1_9NOSO 
ID   A0A367RIX1_9NOSO        Unreviewed;      1098 AA.
AC   A0A367RIX1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=AMP-dependent synthetase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A6770_15910 {ECO:0000313|EMBL:RCJ36508.1};
OS   Nostoc minutum NIES-26.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1844469 {ECO:0000313|EMBL:RCJ36508.1, ECO:0000313|Proteomes:UP000252107};
RN   [1] {ECO:0000313|Proteomes:UP000252107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tabuchi Yagui T.R.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:RCJ36508.1}.
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DR   EMBL; LXQD01000142; RCJ36508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367RIX1; -.
DR   Proteomes; UP000252107; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   CDD; cd05931; FAAL; 1.
DR   CDD; cd06454; KBL_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR22754:SF32; DISCO-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252107};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          24..422
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          609..674
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|Pfam:PF00550"
FT   DOMAIN          739..1082
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   1098 AA;  121710 MW;  14945F3F0B4AC55C CRC64;
     MTIVDSGIKS DFLVPGKTLI DLLHQRVKQQ PHHEAYIFLQ DGEIETNRLT YQELESQVKA
     IAAHLQSLGS PGDRALLLYP PGLDFIAGFF ACLYAGIVAV PAYPPKRNQK LSRLQAIVRD
     ARATLLLTTA EMFQVIEQYG TNEPTFKQLH WVLSDRIATP ARDFIPVTVE SNSLALLQYT
     SGSTGTPKGV MVSHGNLMHN CTAILQFLGK TPNVGFSWLP PYHDMGLIGG ILQPVSGGFT
     GIFMPPMAFL QNPMRWLKGI STYKATVSGG PNFAYDLCVQ NIKSEQLENL DLSSWEIALN
     GAEPIRSETI ESFTKLFSTY GFRLSSFQTC YGMAETTLLV TGVKKAEVPT IKVCDTKALE
     QNQVVSCTAT DVDRGQRKLV SCGHPWLNQT VAIVDPVSLT ECETGQVGEI WVAGESVAQG
     YWNRAEETQK TFGAYFADSG EGPFLRTGDL GFWQDEAGLF VTGRLKDLLV IRGRNHYPQD
     IEQTVETSHP GLGFHSSAAF TVEMDGSDRL IVVCEVKRTY LRNLDAKEVV KTIRQSVLRE
     HELQVYRVLL LKPGTLPKTS SGKIQRFACR ENFLAGNLSL VTSESPDIPQ PIHLNEYPQH
     YSVESIQDWI SQWLATKLNI PMQSINQKES FETYGLDSMQ VAQFIQDLQA WSGYLANIST
     LQTFGAIATF AQYLAQELAR QNNQALTEIP PEYYQFECFP EYAQLQQRLT HIQTLEIPNP
     YFQMQESLTR DCTQVQGRTL INYSTYNYLG LSGDPAVSAA AKDAIDRYGT SVGASRLASG
     ELLLHRELEQ EIAEFIGVED CIVYVSGHAT NVTTIGHLFN SQDLIFYDAL SHNSILQGCS
     LSRAKAIPFP HNDWQALDEM LKDQRQHYRR VLIVIEGIYS MDGDIPELPR FTELKQRHKA
     LLMVDEAHSI GVLGQQGRGI SEFFGVQPAD VDLWMGTLSK AFASCGGYIA GSKALVNYLK
     YTVPGFVYSV GLSPANTAAA LAALRLLKAD PTRVKTLHQR SQHFLTLAKA KGWNTATSQN
     SPIIPIVLGN SLTCIQLSHI LFQAGINVQP IIYPAVANHA ARLRFFISSL HTEEQINATI
     AALAIAFTQV PHIDAENV
//
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