ID B0TX26_FRAP2 Unreviewed; 998 AA.
AC B0TX26;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Non-ribosomal peptide synthetase/alpha-aminoadipate reductase and related {ECO:0000313|EMBL:ABZ87284.1};
GN OrderedLocusNames=Fphi_1061 {ECO:0000313|EMBL:ABZ87284.1};
OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS O#319-036).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=484022 {ECO:0000313|EMBL:ABZ87284.1};
RN [1] {ECO:0000313|EMBL:ABZ87284.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 25017 {ECO:0000313|EMBL:ABZ87284.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Richardson P.;
RT "Complete sequence of chromosome of Francisella philomiragia subsp.
RT philomiragia ATCC 25017.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000937; ABZ87284.1; -; Genomic_DNA.
DR AlphaFoldDB; B0TX26; -.
DR KEGG; fph:Fphi_1061; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_17_6; -.
DR CDD; cd05235; SDR_e1; 1.
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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
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 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; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 548..624
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 998 AA; 113566 MW; CBB03F544B06A248 CRC64;
MILYLSSSAK SFNIVINTHI NTLKIVIPNT LSNCFFIQAK QTPNNIAITD ENIELTYQQT
ANQIINLTRY LSENGYNQNS IISIYSSKRY EIIIAFLAVS SIGASCVQLD KSFPLPLLKD
IINDTNSDLI LCDEIPDIKS VKCIDYINII SKCDDSKIQV PIDINTDPEK DFWLVYSSGT
TGKNKGISIS HRAILESYKI RETIKPYDSG SSIGCNIYYL WEAFRPLLKG GRTNIIPDTV
LYDFKALAKY IKNKKINEIL FTPSYLETLL STSEDTAIEI FNNIDTCWLN GEVVSSWLQY
KLEKFMSSTN IYNLYSISEC HDVAVYKLHP NDKYLKEDGV VPVGHVLPKV DAVVLNENKE
IVKNGQKGEV YIHSIGLANE YINRPDLNAE RFITAANSPI KKRLYKTGDF GKLSDDGQLI
TIYGRCDYII KLRGYTLSLP FIESVIKDKL DIMHCIVDKI GATRMSESLI AYLEIPKENQ
DTFRQRWNLK DNNKPSKKLL DKIAPYLAHY MLPKYIVLLD EIPLNRYSNK LDRNSIKHDD
LIIETQEVQS INNLQDYKRL WSNILNISED DISLTSCFFE LGGSSLSTML LISNLKELGF
DITISNFVEK NSLKDSYNLI TNNQSSTKQK ITPEIFDDIN KFTTAIKPNI CQDLPSTNTG
NILLTGATGF LGSHLVAQLI SNKKIQTIYC LVRATDKNQA RQRVEKTLKK LDVKTNSKIV
YLNGDITKTN FGLDSKKWLE LSKEINTVIH TAASVNLLLP YNALKPSNLD GTAHCIDFCL
TNKSKHLIYI STNGIFPLHL NKVFDESNSI DWIESLESGY SQTKWAAEKL VHKVIEKGLN
ASILRLGNIS PQTPSYINKS DTNWLLLKEI ITQKKIPQNI NLEMTPVDHI TKIVEHLILT
KPDYNTLNIT NKNFLNANIL AKCFNYETIE YNNWLDAIID GSTKFLAKDK LNIDSSICNY
DRTNYQRIMK EININYPEIT AEYINNIFLG DKDEPTYK
//
