ID A0A1I3EIA6_9RHOB Unreviewed; 939 AA.
AC A0A1I3EIA6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II {ECO:0000313|EMBL:SFH98725.1};
GN ORFNames=SAMN04488021_14913 {ECO:0000313|EMBL:SFH98725.1};
OS Paracoccus aminovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34004 {ECO:0000313|EMBL:SFH98725.1, ECO:0000313|Proteomes:UP000183635};
RN [1] {ECO:0000313|EMBL:SFH98725.1, ECO:0000313|Proteomes:UP000183635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8537 {ECO:0000313|EMBL:SFH98725.1,
RC ECO:0000313|Proteomes:UP000183635};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOPU01000049; SFH98725.1; -; Genomic_DNA.
DR RefSeq; WP_074970674.1; NZ_LN832562.1.
DR AlphaFoldDB; A0A1I3EIA6; -.
DR STRING; 34004.SAMN04488021_14913; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000183635; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:SFH98725.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000183635}.
FT DOMAIN 515..597
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 939 AA; 100276 MW; D007F9D0E09F0EE9 CRC64;
MSQTFSSIAD ELAAALPRFS KRIALRDRGL SLSYAQLADF VAAAQPVLAG QQAVAVYGVP
GALFGAAATA CVIDGRPFVH LDPAMPKAVL GNIVSELGIG LILTAEPPKP DQLPPECRVV
DAAGLLGRPA AAPVRAAPVR PSDAIYLVAT SGTTGRPKCI PVTHDAALLS YHWREEYAPY
APGMRVGIYI FAIWEMFRPL RHGAELCFPA LQELLSPQGF TAFLSDHRID EMLFTPSFLE
RILGPVEAGV AAALPLRRVI LNGEVVSDAL IAQLREKLPQ AQLWNLYSIC ETHDICMSEL
RGPAAGKAGV TVGKAMPHLR AVVLDDHDRP CPSGVPGLLH FEGPRMLGPG YVDRPEETAR
RFRELVLEGR AVRLYDTGDQ GFVDEDGEIT VLGRVAHMLK LRGHSIQTAE LTQTLAGVLG
FGKAIPWVVQ VGDQGQMLVF YYTADAAQQA GNAARWQIGP GQQRLPEALA QALRAVLPSY
CLPSYLVQLE TIPIHEVSGK CDYKALPAIA VPAGPERTAD DRAVLPVIAH VARALHCGPD
QIDPARTFHE LGGDSLMGVD LVLALEASYG RRVDFDWALN LPLARLHALL TQTQGVAAAV
AGGFDRPGIL LTGVTGFLGG HVLAAALAQL PPEQVVYCLI RPRNLDPQAR LDRIARALDL
DRQRLVAVGG SIDAPQFGLD DAAYAALCRS SRSVVHCAAT VNLAVDRDHM EAWSRAGIRT
VLDFCRDAGA DLRFSSSSAV FPETGGPYPE ALARLYEGCS GYGAAKIAAE AQIAGSGIPA
AVVRLPSLYD LDAPNPKDIC EIILQACRAM GAMPRGLAFP MTDVRAAAKF LVGLPAPQGV
AFYNLIADQP IAPGEELSPL PPETWLETAP LPEPVRRLIA ADPQILRADA RFRNDAARSA
WSQADGADFA RISDGAALLA RRRLGQNAGQ HAAKESTLP
//
