ID R5Z4I0_9MOLU Unreviewed; 727 AA.
AC R5Z4I0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phosphoglycerate mutase family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN735_00869 {ECO:0000313|EMBL:CDA23712.1};
OS Mycoplasma sp. CAG:611.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1262905 {ECO:0000313|EMBL:CDA23712.1, ECO:0000313|Proteomes:UP000018049};
RN [1] {ECO:0000313|EMBL:CDA23712.1, ECO:0000313|Proteomes:UP000018049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:611 {ECO:0000313|Proteomes:UP000018049};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDA23712.1}.
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DR EMBL; CBBK010000092; CDA23712.1; -; Genomic_DNA.
DR AlphaFoldDB; R5Z4I0; -.
DR STRING; 1262905.BN735_00869; -.
DR Proteomes; UP000018049; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018049};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT BINDING 540..547
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 593
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 727 AA; 84707 MW; A371A8C1F855EBA2 CRC64;
MIEKKEIKNI DCNIENVFNY PEMYIDLINK QKGLVKIDKK KYTGKSLVLV MFTSVCDVGC
PFCCFKALSS ATKKNIKNQF TPEGVNKFIE FANKANVGYL QISGGGEPFL EKEALLKSIE
KINADRIILV TGGVWAYNRE KAEKYLDEIN QAIKKRKKKA RISIRLSISQ CHSIKLKHYP
LENLINIFET KYRDNKNFTL QIKTFKDDPT LENNLKTMGR KFKIEKLQPN KSDDDKIIKI
MPWKSKLILD SGFEIVIGIS RVFYPSFRPN LHNNKSFMKM VELYDIDLDK SQNYFPSRAY
NSKGYFGLDW LVEYNGNIST WQNSIQDDQL NIYEDNYKTS LNHTLANLIT RSCIDNGSKY
REKIVSEISP KTVMLMKANG IRDYASSILF ADAKIRLYAY IRILQDYVKQ GLVNEKLIEN
MPASIQKLIK SPKSVIKKYY LKSNTSILAQ ELSAEPDRDK YKDFLELVKL GHFEMSKQDI
QTAVAYYNMF FPDKRIAKIE DFVNDNKNMD FRLRDRLSPM KKLKDLNNKV NNKKEIYIFR
HGETNWNVEN KIRGTFEDTS LKFTDKGLKQ IDKIALALEK NKIEYIYSSD LIRTRKTVEL
ANKDFKIPVS FHKELRAWNV GKYQGKPLSN FLNSHEGKEA ITDYNKVVTD GESINQVRER
LMYFLEKYVV NCPYERVAII THGATMSNLK SEIDGEQYID IDYCKIVYEN KKFKLVESKI
SETDFAK
//